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a tool for identifying drug-targetable redox-active disulphides

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Lactotransferrin

Intermolecular
Cysteine 424 and cysteine 703 L
Intramolecular
Cysteine 28 and cysteine 64
Cysteine 502 and cysteine 696
Cysteine 646 and cysteine 651
Cysteine 250 and cysteine 264
Cysteine 594 and cysteine 608
Cysteine 377 and cysteine 390
Cysteine 38 and cysteine 55
Cysteine 38 and cysteine 55
Cysteine 377 and cysteine 390
More...
Cysteine 189 and cysteine 200
Cysteine 523 and cysteine 536
Cysteine 424 and cysteine 705 L
Cysteine 446 and cysteine 668
Cysteine 367 and cysteine 399
Cysteine 444 and cysteine 666
Cysteine 510 and cysteine 524
Cysteine 28 and cysteine 64
Cysteine 166 and cysteine 189
Cysteine 510 and cysteine 524
Cysteine 179 and cysteine 202
Cysteine 134 and cysteine 217
Cysteine 176 and cysteine 192
Cysteine 478 and cysteine 553
Cysteine 512 and cysteine 526
Cysteine 192 and cysteine 200
Cysteine 463 and cysteine 538
Cysteine 179 and cysteine 202
Cysteine 179 and cysteine 202
Cysteine 524 and cysteine 534
Cysteine 526 and cysteine 536
Cysteine 523 and cysteine 526
Cysteine 521 and cysteine 524
Cysteine 189 and cysteine 192
Cysteine 497 and cysteine 538
Cysteine 176 and cysteine 200
Cysteine 510 and cysteine 534
Cysteine 512 and cysteine 536
Cysteine 176 and cysteine 217
Cysteine 512 and cysteine 553
A redox-regulated disulphide may form between two units of Lactotransferrin at cysteines 424 and 703 (405 and 684 respectively in this structure).

Details

Redox score ?
86
PDB code
1sdx
Structure name
crystal structure of the zinc saturated c-terminal half of bovine lactoferrin at 2
Structure deposition date
2004-02-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
41
Minimum pKa ?
nan
% buried
nan
Peptide A name
Lactotransferrin
Peptide B name
Lactotransferrin
Peptide A accession
P24627
Peptide B accession
P24627
Peptide A residue number
424
Peptide B residue number
703

Ligandability

Cysteine 424 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 703 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 28 and 64 (1009 and 1045 respectively in this structure).

Details

Redox score ?
89
PDB code
2j4u
Structure name
e
Structure deposition date
2006-09-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9TUM0
Residue number A
28
Residue number B
64
Peptide name
Lactotransferrin

Ligandability

Cysteine 28 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 64 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 502 and 696 (484 and 678 respectively in this structure).

Details

Redox score ?
86
PDB code
2bjj
Structure name
structure of recombinant human lactoferrin produced in the milk of transgenic cows
Structure deposition date
2005-02-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
40
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02788
Residue number A
502
Residue number B
696
Peptide name
Lactotransferrin

Ligandability

Cysteine 502 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 696 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 646 and 651 (627 and 632 respectively in this structure).

Details

Redox score ?
86
PDB code
1fck
Structure name
structure of diceric human lactoferrin
Structure deposition date
2000-07-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02788
Residue number A
646
Residue number B
651
Peptide name
Lactotransferrin

Ligandability

Cysteine 646 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 651 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 250 and 264 (231 and 245 respectively in this structure).

Details

Redox score ?
84
PDB code
1n76
Structure name
crystal structure of human seminal lactoferrin at 3
Structure deposition date
2002-11-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02788
Residue number A
250
Residue number B
264
Peptide name
Lactotransferrin

Ligandability

Cysteine 250 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 264 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 594 and 608 (575 and 589 respectively in this structure).

Details

Redox score ?
84
PDB code
1sqy
Structure name
structure of human diferric lactoferrin at 2
Structure deposition date
2004-03-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02788
Residue number A
594
Residue number B
608
Peptide name
Lactotransferrin

Ligandability

Cysteine 594 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 608 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 377 and 390 (1358 and 1371 respectively in this structure).

Details

Redox score ?
83
PDB code
1cb6
Structure name
structure of human apolactoferrin at 2
Structure deposition date
1999-03-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02788
Residue number A
377
Residue number B
390
Peptide name
Lactotransferrin

Ligandability

Cysteine 377 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 390 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 38 and 55 (19 and 36 respectively in this structure).

Details

Redox score ?
83
PDB code
1h43
Structure name
r210e n-terminal lobe human lactoferrin
Structure deposition date
2002-10-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02788
Residue number A
38
Residue number B
55
Peptide name
Lactotransferrin

Ligandability

Cysteine 38 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 55 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 38 and 55 (19 and 36 respectively in this structure).

Details

Redox score ?
83
PDB code
1biy
Structure name
structure of diferric buffalo lactoferrin
Structure deposition date
1998-06-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
O77698
Residue number A
38
Residue number B
55
Peptide name
Lactotransferrin

Ligandability

Cysteine 38 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 55 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 377 and 390 (358 and 371 respectively in this structure).

Details

Redox score ?
83
PDB code
1dtz
Structure name
structure of camel apo-lactoferrin demonstrates its dual role in sequestering and transporting ferric ions simultaneously:crystal structure of camel apo-lactoferrin at 2
Structure deposition date
2000-01-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9TUM0
Residue number A
377
Residue number B
390
Peptide name
Lactotransferrin

Ligandability

Cysteine 377 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 390 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 189 and 200 (170 and 181 respectively in this structure).

Details

Redox score ?
82
PDB code
1l5t
Structure name
crystal structure of a domain-opened mutant (r121d) of the human lactoferrin n-lobe refined from a merohedrally-twinned crystal form
Structure deposition date
2002-03-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02788
Residue number A
189
Residue number B
200
Peptide name
Lactotransferrin

Ligandability

Cysteine 189 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 200 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 523 and 536 (504 and 517 respectively in this structure).

Details

Redox score ?
82
PDB code
1b0l
Structure name
recombinant human diferric lactoferrin
Structure deposition date
1998-11-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02788
Residue number A
523
Residue number B
536
Peptide name
Lactotransferrin

Ligandability

Cysteine 523 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 536 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 424 and 705 (405 and 686 respectively in this structure).

Details

Redox score ?
82
PDB code
1n76
Structure name
crystal structure of human seminal lactoferrin at 3
Structure deposition date
2002-11-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02788
Residue number A
424
Residue number B
705
Peptide name
Lactotransferrin

Ligandability

Cysteine 424 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 705 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 446 and 668 (427 and 649 respectively in this structure).

Details

Redox score ?
81
PDB code
1fck
Structure name
structure of diceric human lactoferrin
Structure deposition date
2000-07-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02788
Residue number A
446
Residue number B
668
Peptide name
Lactotransferrin

Ligandability

Cysteine 446 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 668 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 367 and 399 (348 and 380 respectively in this structure).

Details

Redox score ?
81
PDB code
1lcf
Structure name
crystal structure of copper-and oxalate-substituted human lactoferrin at 2
Structure deposition date
1994-01-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02788
Residue number A
367
Residue number B
399
Peptide name
Lactotransferrin

Ligandability

Cysteine 367 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 399 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 444 and 666 (425 and 647 respectively in this structure).

Details

Redox score ?
81
PDB code
1biy
Structure name
structure of diferric buffalo lactoferrin
Structure deposition date
1998-06-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
O77698
Residue number A
444
Residue number B
666
Peptide name
Lactotransferrin

Ligandability

Cysteine 444 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 666 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 510 and 524 (491 and 505 respectively in this structure).

Details

Redox score ?
80
PDB code
1jw1
Structure name
crystallization and structure determination of goat lactoferrin at 4
Structure deposition date
2001-09-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
97
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q29477
Residue number A
510
Residue number B
524
Peptide name
Lactotransferrin

Ligandability

Cysteine 510 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 524 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 28 and 64 (9 and 45 respectively in this structure).

Details

Redox score ?
80
PDB code
1bka
Structure name
oxalate-substituted diferric lactoferrin
Structure deposition date
1996-04-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02788
Residue number A
28
Residue number B
64
Peptide name
Lactotransferrin

Ligandability

Cysteine 28 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 64 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 166 and 189 (160 and 183 respectively in this structure).

Details

Redox score ?
80
PDB code
1i6b
Structure name
structure of equine apolactoferrin at 3
Structure deposition date
2001-03-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
O77811
Residue number A
166
Residue number B
189
Peptide name
Lactotransferrin

Ligandability

Cysteine 166 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 189 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 510 and 524 (491 and 505 respectively in this structure).

Details

Redox score ?
79
PDB code
1i6q
Structure name
formation of a protein intermediate and its trapping by the simultaneous crystallization process: crystal structure of an iron-saturated intermediate in the fe3+ binding pathway of camel lactoferrin at 2
Structure deposition date
2001-03-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
101
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9TUM0
Residue number A
510
Residue number B
524
Peptide name
Lactotransferrin

Ligandability

Cysteine 510 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 524 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 179 and 202 (160 and 183 respectively in this structure).

Details

Redox score ?
79
PDB code
1dtz
Structure name
structure of camel apo-lactoferrin demonstrates its dual role in sequestering and transporting ferric ions simultaneously:crystal structure of camel apo-lactoferrin at 2
Structure deposition date
2000-01-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9TUM0
Residue number A
179
Residue number B
202
Peptide name
Lactotransferrin

Ligandability

Cysteine 179 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 202 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 134 and 217 (1115 and 1198 respectively in this structure).

Details

Redox score ?
79
PDB code
1cb6
Structure name
structure of human apolactoferrin at 2
Structure deposition date
1999-03-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
89
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02788
Residue number A
134
Residue number B
217
Peptide name
Lactotransferrin

Ligandability

Cysteine 134 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 217 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 176 and 192 (1157 and 1173 respectively in this structure).

Details

Redox score ?
79
PDB code
1cb6
Structure name
structure of human apolactoferrin at 2
Structure deposition date
1999-03-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
100
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02788
Residue number A
176
Residue number B
192
Peptide name
Lactotransferrin

Ligandability

Cysteine 176 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 192 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 478 and 553 (459 and 534 respectively in this structure).

Details

Redox score ?
79
PDB code
1n76
Structure name
crystal structure of human seminal lactoferrin at 3
Structure deposition date
2002-11-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
91
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02788
Residue number A
478
Residue number B
553
Peptide name
Lactotransferrin

Ligandability

Cysteine 478 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 553 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 512 and 526 (493 and 507 respectively in this structure).

Details

Redox score ?
78
PDB code
1b0l
Structure name
recombinant human diferric lactoferrin
Structure deposition date
1998-11-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
101
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02788
Residue number A
512
Residue number B
526
Peptide name
Lactotransferrin

Ligandability

Cysteine 512 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 526 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 192 and 200 (173 and 181 respectively in this structure).

Details

Redox score ?
78
PDB code
1lfi
Structure name
metal substitution in transferrins: the crystal structure of human copper-lactoferrin at 2
Structure deposition date
1992-02-10
Thiol separation (Å)
3
Half-sphere exposure sum ?
89
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02788
Residue number A
192
Residue number B
200
Peptide name
Lactotransferrin

Ligandability

Cysteine 192 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 200 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 463 and 538 (457 and 532 respectively in this structure).

Details

Redox score ?
78
PDB code
1b1x
Structure name
structure of diferric mare lactoferrin at 2
Structure deposition date
1998-11-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
92
Minimum pKa ?
nan
% buried
nan
Peptide accession
O77811
Residue number A
463
Residue number B
538
Peptide name
Lactotransferrin

Ligandability

Cysteine 463 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 538 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 179 and 202 (160 and 183 respectively in this structure).

Details

Redox score ?
77
PDB code
1blf
Structure name
structure of diferric bovine lactoferrin at 2
Structure deposition date
1997-08-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P24627
Residue number A
179
Residue number B
202
Peptide name
Lactotransferrin

Ligandability

Cysteine 179 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 202 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 179 and 202 (160 and 183 respectively in this structure).

Details

Redox score ?
77
PDB code
1biy
Structure name
structure of diferric buffalo lactoferrin
Structure deposition date
1998-06-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
O77698
Residue number A
179
Residue number B
202
Peptide name
Lactotransferrin

Ligandability

Cysteine 179 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 202 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 524 and 534 (505 and 515 respectively in this structure).

Details

Redox score ?
76
PDB code
1dtz
Structure name
structure of camel apo-lactoferrin demonstrates its dual role in sequestering and transporting ferric ions simultaneously:crystal structure of camel apo-lactoferrin at 2
Structure deposition date
2000-01-13
Thiol separation (Å)
3
Half-sphere exposure sum ?
91
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9TUM0
Residue number A
524
Residue number B
534
Peptide name
Lactotransferrin

Ligandability

Cysteine 524 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 534 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 526 and 536 (507 and 517 respectively in this structure).

Details

Redox score ?
75
PDB code
1lcf
Structure name
crystal structure of copper-and oxalate-substituted human lactoferrin at 2
Structure deposition date
1994-01-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02788
Residue number A
526
Residue number B
536
Peptide name
Lactotransferrin

Ligandability

Cysteine 526 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 536 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 523 and 526 (504 and 507 respectively in this structure).

Details

Redox score ?
67
PDB code
1lfg
Structure name
structure of diferric human lactoferrin
Structure deposition date
1992-02-05
Thiol separation (Å)
5
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02788
Residue number A
523
Residue number B
526
Peptide name
Lactotransferrin

Ligandability

Cysteine 523 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 526 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 521 and 524 (502 and 505 respectively in this structure).

Details

Redox score ?
66
PDB code
1i6q
Structure name
formation of a protein intermediate and its trapping by the simultaneous crystallization process: crystal structure of an iron-saturated intermediate in the fe3+ binding pathway of camel lactoferrin at 2
Structure deposition date
2001-03-03
Thiol separation (Å)
5
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9TUM0
Residue number A
521
Residue number B
524
Peptide name
Lactotransferrin

Ligandability

Cysteine 521 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 524 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 189 and 192 (170 and 173 respectively in this structure).

Details

Redox score ?
66
PDB code
1lfg
Structure name
structure of diferric human lactoferrin
Structure deposition date
1992-02-05
Thiol separation (Å)
5
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02788
Residue number A
189
Residue number B
192
Peptide name
Lactotransferrin

Ligandability

Cysteine 189 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 192 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 497 and 538 (491 and 532 respectively in this structure).

Details

Redox score ?
65
PDB code
1qjm
Structure name
crystal structure of a complex of lactoferrin with a lanthanide ion (sm3+) at 3
Structure deposition date
1999-06-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
94
Minimum pKa ?
nan
% buried
nan
Peptide accession
O77811
Residue number A
497
Residue number B
538
Peptide name
Lactotransferrin

Ligandability

Cysteine 497 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 538 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 176 and 200 (157 and 181 respectively in this structure).

Details

Redox score ?
63
PDB code
1lfi
Structure name
metal substitution in transferrins: the crystal structure of human copper-lactoferrin at 2
Structure deposition date
1992-02-10
Thiol separation (Å)
5
Half-sphere exposure sum ?
95
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02788
Residue number A
176
Residue number B
200
Peptide name
Lactotransferrin

Ligandability

Cysteine 176 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 200 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 510 and 534 (491 and 515 respectively in this structure).

Details

Redox score ?
61
PDB code
3usd
Structure name
crystal structure of c-lobe of bovine lactoferrin complexed with imidazol (1,2 a) pyridine3-yl-acitic acid at 2
Structure deposition date
2011-11-23
Thiol separation (Å)
5
Half-sphere exposure sum ?
94
Minimum pKa ?
nan
% buried
nan
Peptide accession
P24627
Residue number A
510
Residue number B
534
Peptide name
Lactotransferrin

Ligandability

Cysteine 510 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 534 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 512 and 536 (493 and 517 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
1sqy
Structure name
structure of human diferric lactoferrin at 2
Structure deposition date
2004-03-22
Thiol separation (Å)
5
Half-sphere exposure sum ?
93
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02788
Residue number A
512
Residue number B
536
Peptide name
Lactotransferrin

Ligandability

Cysteine 512 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 536 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 176 and 217 (157 and 198 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
1lfh
Structure name
molecular replacement solution of the structure of apolactoferrin, a protein displaying large-scale conformational change
Structure deposition date
1991-09-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
91
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02788
Residue number A
176
Residue number B
217
Peptide name
Lactotransferrin

Ligandability

Cysteine 176 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 217 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lactotransferrin between cysteines 512 and 553 (493 and 534 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
1sqy
Structure name
structure of human diferric lactoferrin at 2
Structure deposition date
2004-03-22
Thiol separation (Å)
6
Half-sphere exposure sum ?
92
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02788
Residue number A
512
Residue number B
553
Peptide name
Lactotransferrin

Ligandability

Cysteine 512 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 553 of Lactotransferrin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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