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Complement component C8 beta chain

Intramolecular
Cysteine 557 and cysteine 590
Cysteine 79 and cysteine 116
Cysteine 76 and cysteine 110
Cysteine 65 and cysteine 100
Cysteine 122 and cysteine 133
Cysteine 140 and cysteine 155 L
Cysteine 525 and cysteine 534
Cysteine 508 and cysteine 523
Cysteine 127 and cysteine 146 L
Cysteine 505 and cysteine 521
More...
Cysteine 503 and cysteine 550
Cysteine 162 and cysteine 200
Cysteine 378 and cysteine 403
Cysteine 521 and cysteine 523
Cysteine 523 and cysteine 525
Cysteine 523 and cysteine 534
Cysteine 508 and cysteine 521
Cysteine 508 and cysteine 525
Cysteine 122 and cysteine 127 L
Cysteine 508 and cysteine 534
Cysteine 505 and cysteine 508
Cysteine 505 and cysteine 523
Cysteine 550 and cysteine 568
Cysteine 127 and cysteine 133 L
Cysteine 503 and cysteine 568
Cysteine 505 and cysteine 568
Cysteine 505 and cysteine 550
Cysteine 503 and cysteine 505
Cysteine 122 and cysteine 146
Cysteine 508 and cysteine 568
Cysteine 521 and cysteine 568
Cysteine 521 and cysteine 534
Cysteine 133 and cysteine 146
A redox-regulated disulphide may form within Complement component C8 beta chain between cysteines 557 and 590 (503 and 536 respectively in this structure).

Details

Redox score ?
90
PDB code
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
557
Residue number B
590
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 557 of Complement component C8 beta chain

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 590 of Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 79 and 116 (25 and 62 respectively in this structure).

Details

Redox score ?
87
PDB code
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
79
Residue number B
116
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 79 of Complement component C8 beta chain

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 116 of Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 76 and 110 (22 and 56 respectively in this structure).

Details

Redox score ?
87
PDB code
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
76
Residue number B
110
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 76 of Complement component C8 beta chain

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 110 of Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 65 and 100 (11 and 46 respectively in this structure).

Details

Redox score ?
86
PDB code
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
65
Residue number B
100
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 65 of Complement component C8 beta chain

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 100 of Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 122 and 133 (68 and 79 respectively in this structure).

Details

Redox score ?
85
PDB code
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
122
Residue number B
133
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 122 of Complement component C8 beta chain

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 133 of Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 140 and 155 (86 and 101 respectively in this structure).

Details

Redox score ?
84
PDB code
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
140
Residue number B
155
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 140 of Complement component C8 beta chain

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 155 of Complement component C8 beta chain

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.

A redox-regulated disulphide may form within Complement component C8 beta chain between cysteines 525 and 534 (471 and 480 respectively in this structure).

Details

Redox score ?
84
PDB code
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
525
Residue number B
534
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 525 of Complement component C8 beta chain

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 Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 508 and 523 (454 and 469 respectively in this structure).

Details

Redox score ?
84
PDB code
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
508
Residue number B
523
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 508 of Complement component C8 beta chain

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 523 of Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 127 and 146 (73 and 92 respectively in this structure).

Details

Redox score ?
83
PDB code
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
127
Residue number B
146
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 127 of Complement component C8 beta chain

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 146 of Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 505 and 521 (451 and 467 respectively in this structure).

Details

Redox score ?
82
PDB code
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
505
Residue number B
521
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 505 of Complement component C8 beta chain

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 521 of Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 503 and 550 (449 and 496 respectively in this structure).

Details

Redox score ?
81
PDB code
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
503
Residue number B
550
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 503 of Complement component C8 beta chain

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 550 of Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 162 and 200 (108 and 146 respectively in this structure).

Details

Redox score ?
76
PDB code
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
5
Half-sphere exposure sum ?
41
Minimum pKa ?
9
% buried
13
Peptide accession
P07358
Residue number A
162
Residue number B
200
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 162 of Complement component C8 beta chain

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 Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 378 and 403 (324 and 349 respectively in this structure).

Details

Redox score ?
75
PDB code
6h04
Structure name
closed conformation of the membrane attack complex
Structure deposition date
2018-07-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
3
Peptide accession
P07358
Residue number A
378
Residue number B
403
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 378 of Complement component C8 beta chain

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 403 of Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 521 and 523 (467 and 469 respectively in this structure).

Details

Redox score ?
60
PDB code
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
6
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
521
Residue number B
523
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 521 of Complement component C8 beta chain

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 523 of Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 523 and 525 (469 and 471 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
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
6
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
523
Residue number B
525
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 523 of Complement component C8 beta chain

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 Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 523 and 534 (469 and 480 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
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
523
Residue number B
534
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 523 of Complement component C8 beta chain

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 Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 508 and 521 (454 and 467 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
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
508
Residue number B
521
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 508 of Complement component C8 beta chain

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 521 of Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 508 and 525 (454 and 471 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
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
508
Residue number B
525
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 508 of Complement component C8 beta chain

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 Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 122 and 127 (68 and 73 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
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
122
Residue number B
127
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 122 of Complement component C8 beta chain

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 127 of Complement component C8 beta chain

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.

A redox-regulated disulphide may form within Complement component C8 beta chain between cysteines 508 and 534 (454 and 480 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
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
508
Residue number B
534
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 508 of Complement component C8 beta chain

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 Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 505 and 508 (451 and 454 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
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
505
Residue number B
508
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 505 of Complement component C8 beta chain

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 508 of Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 505 and 523 (451 and 469 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
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
505
Residue number B
523
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 505 of Complement component C8 beta chain

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 523 of Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 550 and 568 (496 and 514 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
nan
Peptide accession
P07358
Residue number A
550
Residue number B
568
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 550 of Complement component C8 beta chain

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 568 of Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 127 and 133 (73 and 79 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
127
Residue number B
133
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 127 of Complement component C8 beta chain

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 133 of Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 503 and 568 (449 and 514 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
nan
Peptide accession
P07358
Residue number A
503
Residue number B
568
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 503 of Complement component C8 beta chain

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 568 of Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 505 and 568 (451 and 514 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
nan
Peptide accession
P07358
Residue number A
505
Residue number B
568
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 505 of Complement component C8 beta chain

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 568 of Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 505 and 550 (451 and 496 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
505
Residue number B
550
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 505 of Complement component C8 beta chain

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 550 of Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 503 and 505 (449 and 451 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
503
Residue number B
505
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 503 of Complement component C8 beta chain

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 505 of Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 122 and 146 (68 and 92 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
122
Residue number B
146
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 122 of Complement component C8 beta chain

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 146 of Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 508 and 568 (454 and 514 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
nan
Peptide accession
P07358
Residue number A
508
Residue number B
568
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 508 of Complement component C8 beta chain

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 568 of Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 521 and 568 (467 and 514 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
nan
Peptide accession
P07358
Residue number A
521
Residue number B
568
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 521 of Complement component C8 beta chain

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 568 of Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 521 and 534 (467 and 480 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
521
Residue number B
534
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 521 of Complement component C8 beta chain

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 Complement component C8 beta chain

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 Complement component C8 beta chain between cysteines 133 and 146 (79 and 92 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
3ojy
Structure name
crystal structure of human complement component c8
Structure deposition date
2010-08-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07358
Residue number A
133
Residue number B
146
Peptide name
Complement component C8 beta chain

Ligandability

Cysteine 133 of Complement component C8 beta chain

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 146 of Complement component C8 beta chain

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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