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a tool for identifying drug-targetable redox-active disulphides

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Serotransferrin

Intramolecular
Cysteine 634 and cysteine 639
Cysteine 358 and cysteine 615
Cysteine 156 and cysteine 350
Cysteine 493 and cysteine 684
Cysteine 582 and cysteine 596
Cysteine 246 and cysteine 260
Cysteine 514 and cysteine 525
Cysteine 246 and cysteine 260
Cysteine 374 and cysteine 387
Cysteine 501 and cysteine 515
More...
Cysteine 436 and cysteine 653
Cysteine 190 and cysteine 196
Cysteine 38 and cysteine 58
Cysteine 421 and cysteine 693
Cysteine 28 and cysteine 67
Cysteine 364 and cysteine 396
Cysteine 170 and cysteine 181
Cysteine 437 and cysteine 656
Cysteine 503 and cysteine 517
Cysteine 177 and cysteine 193
Cysteine 469 and cysteine 542
Cysteine 137 and cysteine 213
Cysteine 180 and cysteine 198
Cysteine 160 and cysteine 183
Cysteine 517 and cysteine 525
Cysteine 504 and cysteine 515
Cysteine 173 and cysteine 181
Cysteine 193 and cysteine 196
Cysteine 514 and cysteine 517
Cysteine 177 and cysteine 213
Cysteine 177 and cysteine 196
Cysteine 503 and cysteine 525
Cysteine 503 and cysteine 542
Cysteine 490 and cysteine 515
Cysteine 157 and cysteine 181
Cysteine 517 and cysteine 542
Cysteine 190 and cysteine 193
Cysteine 177 and cysteine 190
Cysteine 137 and cysteine 177
Cysteine 503 and cysteine 514
A redox-regulated disulphide may form within Serotransferrin between cysteines 634 and 639 (615 and 620 respectively in this structure).

Details

Redox score ?
86
PDB code
3skp
Structure name
the structure of apo-human transferrin c-lobe with bound sulfate ions
Structure deposition date
2011-06-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
634
Residue number B
639
Peptide name
Serotransferrin

Ligandability

Cysteine 634 of Serotransferrin

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 639 of Serotransferrin

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 Serotransferrin between cysteines 358 and 615 (339 and 596 respectively in this structure).

Details

Redox score ?
86
PDB code
2hav
Structure name
apo-human serum transferrin (glycosylated)
Structure deposition date
2006-06-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
358
Residue number B
615
Peptide name
Serotransferrin

Ligandability

Cysteine 358 of Serotransferrin

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 615 of Serotransferrin

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 Serotransferrin between cysteines 156 and 350 (137 and 331 respectively in this structure).

Details

Redox score ?
86
PDB code
3v8x
Structure name
the crystal structure of transferrin binding protein a (tbpa) from neisserial meningitidis serogroup b in complex with full length human transferrin
Structure deposition date
2011-12-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
156
Residue number B
350
Peptide name
Serotransferrin

Ligandability

Cysteine 156 of Serotransferrin

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 350 of Serotransferrin

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 Serotransferrin between cysteines 493 and 684 (474 and 665 respectively in this structure).

Details

Redox score ?
85
PDB code
3ve1
Structure name
the 2
Structure deposition date
2012-01-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
493
Residue number B
684
Peptide name
Serotransferrin

Ligandability

Cysteine 493 of Serotransferrin

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 684 of Serotransferrin

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 Serotransferrin between cysteines 582 and 596 (563 and 577 respectively in this structure).

Details

Redox score ?
84
PDB code
3v83
Structure name
the 2
Structure deposition date
2011-12-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
582
Residue number B
596
Peptide name
Serotransferrin

Ligandability

Cysteine 582 of Serotransferrin

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 596 of Serotransferrin

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 Serotransferrin between cysteines 246 and 260 (227 and 241 respectively in this structure).

Details

Redox score ?
84
PDB code
1jnf
Structure name
rabbit serum transferrin at 2
Structure deposition date
2001-07-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19134
Residue number A
246
Residue number B
260
Peptide name
Serotransferrin

Ligandability

Cysteine 246 of Serotransferrin

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 260 of Serotransferrin

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 Serotransferrin between cysteines 514 and 525 (495 and 506 respectively in this structure).

Details

Redox score ?
83
PDB code
3skp
Structure name
the structure of apo-human transferrin c-lobe with bound sulfate ions
Structure deposition date
2011-06-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
514
Residue number B
525
Peptide name
Serotransferrin

Ligandability

Cysteine 514 of Serotransferrin

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 525 of Serotransferrin

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 Serotransferrin between cysteines 246 and 260 (227 and 241 respectively in this structure).

Details

Redox score ?
83
PDB code
1oqg
Structure name
crystal structure of the d63e mutant of the n-lobe human transferrin
Structure deposition date
2003-03-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
246
Residue number B
260
Peptide name
Serotransferrin

Ligandability

Cysteine 246 of Serotransferrin

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 260 of Serotransferrin

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 Serotransferrin between cysteines 374 and 387 (355 and 368 respectively in this structure).

Details

Redox score ?
83
PDB code
3v89
Structure name
the crystal structure of transferrin binding protein a (tbpa) from neisseria meningitidis serogroup b in complex with the c-lobe of human transferrin
Structure deposition date
2011-12-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
374
Residue number B
387
Peptide name
Serotransferrin

Ligandability

Cysteine 374 of Serotransferrin

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 387 of Serotransferrin

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 Serotransferrin between cysteines 501 and 515.

Details

Redox score ?
83
PDB code
1h76
Structure name
the crystal structure of diferric porcine serum transferrin
Structure deposition date
2001-07-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09571
Residue number A
501
Residue number B
515
Peptide name
Serotransferrin

Ligandability

Cysteine 501 of Serotransferrin

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 515 of Serotransferrin

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 Serotransferrin between cysteines 436 and 653 (417 and 634 respectively in this structure).

Details

Redox score ?
82
PDB code
1jnf
Structure name
rabbit serum transferrin at 2
Structure deposition date
2001-07-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19134
Residue number A
436
Residue number B
653
Peptide name
Serotransferrin

Ligandability

Cysteine 436 of Serotransferrin

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 653 of Serotransferrin

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 Serotransferrin between cysteines 190 and 196 (171 and 177 respectively in this structure).

Details

Redox score ?
82
PDB code
1fqf
Structure name
crystal structures of mutant (k296a) that abolish the dilysine interaction in the n-lobe of human transferrin
Structure deposition date
2000-09-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
190
Residue number B
196
Peptide name
Serotransferrin

Ligandability

Cysteine 190 of Serotransferrin

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 196 of Serotransferrin

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 Serotransferrin between cysteines 38 and 58 (19 and 39 respectively in this structure).

Details

Redox score ?
82
PDB code
1btj
Structure name
human serum transferrin, recombinant n-terminal lobe, apo form, crystal form 2
Structure deposition date
1998-09-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
38
Residue number B
58
Peptide name
Serotransferrin

Ligandability

Cysteine 38 of Serotransferrin

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 58 of Serotransferrin

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 Serotransferrin between cysteines 421 and 693 (402 and 674 respectively in this structure).

Details

Redox score ?
82
PDB code
2hav
Structure name
apo-human serum transferrin (glycosylated)
Structure deposition date
2006-06-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
421
Residue number B
693
Peptide name
Serotransferrin

Ligandability

Cysteine 421 of Serotransferrin

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 693 of Serotransferrin

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 Serotransferrin between cysteines 28 and 67 (9 and 48 respectively in this structure).

Details

Redox score ?
81
PDB code
1d4n
Structure name
human serum transferrin
Structure deposition date
1999-10-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
28
Residue number B
67
Peptide name
Serotransferrin

Ligandability

Cysteine 28 of Serotransferrin

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 67 of Serotransferrin

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 Serotransferrin between cysteines 364 and 396 (345 and 377 respectively in this structure).

Details

Redox score ?
81
PDB code
7q1l
Structure name
glycosilated human serum apo-tranferrin
Structure deposition date
2021-10-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
364
Residue number B
396
Peptide name
Serotransferrin

Ligandability

Cysteine 364 of Serotransferrin

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 396 of Serotransferrin

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 Serotransferrin between cysteines 170 and 181.

Details

Redox score ?
81
PDB code
1h76
Structure name
the crystal structure of diferric porcine serum transferrin
Structure deposition date
2001-07-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09571
Residue number A
170
Residue number B
181
Peptide name
Serotransferrin

Ligandability

Cysteine 170 of Serotransferrin

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 181 of Serotransferrin

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 Serotransferrin between cysteines 437 and 656 (418 and 637 respectively in this structure).

Details

Redox score ?
80
PDB code
3v89
Structure name
the crystal structure of transferrin binding protein a (tbpa) from neisseria meningitidis serogroup b in complex with the c-lobe of human transferrin
Structure deposition date
2011-12-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
437
Residue number B
656
Peptide name
Serotransferrin

Ligandability

Cysteine 437 of Serotransferrin

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 656 of Serotransferrin

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 Serotransferrin between cysteines 503 and 517 (484 and 498 respectively in this structure).

Details

Redox score ?
79
PDB code
3v83
Structure name
the 2
Structure deposition date
2011-12-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
101
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
503
Residue number B
517
Peptide name
Serotransferrin

Ligandability

Cysteine 503 of Serotransferrin

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 517 of Serotransferrin

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 Serotransferrin between cysteines 177 and 193 (158 and 174 respectively in this structure).

Details

Redox score ?
79
PDB code
2hav
Structure name
apo-human serum transferrin (glycosylated)
Structure deposition date
2006-06-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
91
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
177
Residue number B
193
Peptide name
Serotransferrin

Ligandability

Cysteine 177 of Serotransferrin

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 193 of Serotransferrin

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 Serotransferrin between cysteines 469 and 542 (450 and 523 respectively in this structure).

Details

Redox score ?
78
PDB code
3v8x
Structure name
the crystal structure of transferrin binding protein a (tbpa) from neisserial meningitidis serogroup b in complex with full length human transferrin
Structure deposition date
2011-12-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
92
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
469
Residue number B
542
Peptide name
Serotransferrin

Ligandability

Cysteine 469 of Serotransferrin

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 542 of Serotransferrin

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 Serotransferrin between cysteines 137 and 213 (118 and 194 respectively in this structure).

Details

Redox score ?
78
PDB code
6soz
Structure name
glycosylated trypanosoma brucei transferrin receptor in complex with human transferrin
Structure deposition date
2019-08-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
91
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
137
Residue number B
213
Peptide name
Serotransferrin

Ligandability

Cysteine 137 of Serotransferrin

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 213 of Serotransferrin

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 Serotransferrin between cysteines 180 and 198 (161 and 179 respectively in this structure).

Details

Redox score ?
78
PDB code
1n84
Structure name
human serum transferrin, n-lobe
Structure deposition date
2002-11-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
180
Residue number B
198
Peptide name
Serotransferrin

Ligandability

Cysteine 180 of Serotransferrin

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 198 of Serotransferrin

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 Serotransferrin between cysteines 160 and 183.

Details

Redox score ?
77
PDB code
1h76
Structure name
the crystal structure of diferric porcine serum transferrin
Structure deposition date
2001-07-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09571
Residue number A
160
Residue number B
183
Peptide name
Serotransferrin

Ligandability

Cysteine 160 of Serotransferrin

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 183 of Serotransferrin

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 Serotransferrin between cysteines 517 and 525 (498 and 506 respectively in this structure).

Details

Redox score ?
76
PDB code
2hav
Structure name
apo-human serum transferrin (glycosylated)
Structure deposition date
2006-06-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
517
Residue number B
525
Peptide name
Serotransferrin

Ligandability

Cysteine 517 of Serotransferrin

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 525 of Serotransferrin

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 Serotransferrin between cysteines 504 and 515.

Details

Redox score ?
75
PDB code
1h76
Structure name
the crystal structure of diferric porcine serum transferrin
Structure deposition date
2001-07-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09571
Residue number A
504
Residue number B
515
Peptide name
Serotransferrin

Ligandability

Cysteine 504 of Serotransferrin

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 515 of Serotransferrin

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 Serotransferrin between cysteines 173 and 181.

Details

Redox score ?
74
PDB code
1h76
Structure name
the crystal structure of diferric porcine serum transferrin
Structure deposition date
2001-07-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09571
Residue number A
173
Residue number B
181
Peptide name
Serotransferrin

Ligandability

Cysteine 173 of Serotransferrin

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 181 of Serotransferrin

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 Serotransferrin between cysteines 193 and 196 (174 and 177 respectively in this structure).

Details

Redox score ?
71
PDB code
2o7u
Structure name
crystal structure of k206e/k296e mutant of the n-terminal half molecule of human transferrin
Structure deposition date
2006-12-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
193
Residue number B
196
Peptide name
Serotransferrin

Ligandability

Cysteine 193 of Serotransferrin

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 196 of Serotransferrin

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 Serotransferrin between cysteines 514 and 517 (495 and 498 respectively in this structure).

Details

Redox score ?
68
PDB code
2hau
Structure name
apo-human serum transferrin (non-glycosylated)
Structure deposition date
2006-06-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
514
Residue number B
517
Peptide name
Serotransferrin

Ligandability

Cysteine 514 of Serotransferrin

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 517 of Serotransferrin

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 Serotransferrin between cysteines 177 and 213 (158 and 194 respectively in this structure).

Details

Redox score ?
64
PDB code
3s9l
Structure name
complex between transferrin receptor 1 and transferrin with iron in the n-lobe, cryocooled 2
Structure deposition date
2011-06-01
Thiol separation (Å)
5
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
177
Residue number B
213
Peptide name
Serotransferrin

Ligandability

Cysteine 177 of Serotransferrin

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 213 of Serotransferrin

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 Serotransferrin between cysteines 177 and 196 (158 and 177 respectively in this structure).

Details

Redox score ?
62
PDB code
7q1l
Structure name
glycosilated human serum apo-tranferrin
Structure deposition date
2021-10-20
Thiol separation (Å)
5
Half-sphere exposure sum ?
99
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
177
Residue number B
196
Peptide name
Serotransferrin

Ligandability

Cysteine 177 of Serotransferrin

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 196 of Serotransferrin

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 Serotransferrin between cysteines 503 and 525 (484 and 506 respectively in this structure).

Details

Redox score ?
62
PDB code
2hau
Structure name
apo-human serum transferrin (non-glycosylated)
Structure deposition date
2006-06-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
503
Residue number B
525
Peptide name
Serotransferrin

Ligandability

Cysteine 503 of Serotransferrin

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 525 of Serotransferrin

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 Serotransferrin between cysteines 503 and 542 (484 and 523 respectively in this structure).

Details

Redox score ?
60
PDB code
2hav
Structure name
apo-human serum transferrin (glycosylated)
Structure deposition date
2006-06-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
98
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
503
Residue number B
542
Peptide name
Serotransferrin

Ligandability

Cysteine 503 of Serotransferrin

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 542 of Serotransferrin

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 Serotransferrin between cysteines 490 and 515.

Details

Redox score ?
60
PDB code
1h76
Structure name
the crystal structure of diferric porcine serum transferrin
Structure deposition date
2001-07-03
Thiol separation (Å)
5
Half-sphere exposure sum ?
94
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09571
Residue number A
490
Residue number B
515
Peptide name
Serotransferrin

Ligandability

Cysteine 490 of Serotransferrin

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 515 of Serotransferrin

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 Serotransferrin between cysteines 157 and 181. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
1h76
Structure name
the crystal structure of diferric porcine serum transferrin
Structure deposition date
2001-07-03
Thiol separation (Å)
5
Half-sphere exposure sum ?
97
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09571
Residue number A
157
Residue number B
181
Peptide name
Serotransferrin

Ligandability

Cysteine 157 of Serotransferrin

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 181 of Serotransferrin

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 Serotransferrin between cysteines 517 and 542 (498 and 523 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
2hau
Structure name
apo-human serum transferrin (non-glycosylated)
Structure deposition date
2006-06-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
517
Residue number B
542
Peptide name
Serotransferrin

Ligandability

Cysteine 517 of Serotransferrin

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 542 of Serotransferrin

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 Serotransferrin between cysteines 190 and 193 (171 and 174 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
5dyh
Structure name
ti(iv) bound human serum transferrin
Structure deposition date
2015-09-24
Thiol separation (Å)
6
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
190
Residue number B
193
Peptide name
Serotransferrin

Ligandability

Cysteine 190 of Serotransferrin

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 193 of Serotransferrin

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 Serotransferrin between cysteines 177 and 190 (158 and 171 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
7q1l
Structure name
glycosilated human serum apo-tranferrin
Structure deposition date
2021-10-20
Thiol separation (Å)
6
Half-sphere exposure sum ?
94
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
177
Residue number B
190
Peptide name
Serotransferrin

Ligandability

Cysteine 177 of Serotransferrin

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 190 of Serotransferrin

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 Serotransferrin between cysteines 137 and 177 (118 and 158 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
5dyh
Structure name
ti(iv) bound human serum transferrin
Structure deposition date
2015-09-24
Thiol separation (Å)
6
Half-sphere exposure sum ?
102
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
137
Residue number B
177
Peptide name
Serotransferrin

Ligandability

Cysteine 137 of Serotransferrin

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 177 of Serotransferrin

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 Serotransferrin between cysteines 503 and 514 (484 and 495 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
2hau
Structure name
apo-human serum transferrin (non-glycosylated)
Structure deposition date
2006-06-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02787
Residue number A
503
Residue number B
514
Peptide name
Serotransferrin

Ligandability

Cysteine 503 of Serotransferrin

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 514 of Serotransferrin

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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