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Complement component C8 alpha chain

Intermolecular
Cysteine 194 and cysteine 60 of Complement component C8 gamma chain
Intramolecular
Cysteine 551 and cysteine 584
Cysteine 562 and cysteine 574
Cysteine 53 and cysteine 90
Cysteine 39 and cysteine 74
Cysteine 50 and cysteine 84
Cysteine 502 and cysteine 517
Cysteine 115 and cysteine 130
Cysteine 519 and cysteine 528
Cysteine 102 and cysteine 121
More...
Cysteine 499 and cysteine 515
Cysteine 96 and cysteine 108
Cysteine 375 and cysteine 399
Cysteine 140 and cysteine 177
Cysteine 497 and cysteine 544
Cysteine 517 and cysteine 519
Cysteine 502 and cysteine 519
Cysteine 502 and cysteine 528
Cysteine 517 and cysteine 528
Cysteine 96 and cysteine 102
Cysteine 499 and cysteine 517
Cysteine 515 and cysteine 517
Cysteine 499 and cysteine 544
Cysteine 499 and cysteine 502
Cysteine 96 and cysteine 121
Cysteine 497 and cysteine 499
Cysteine 102 and cysteine 108
Cysteine 515 and cysteine 544
Cysteine 502 and cysteine 515
Cysteine 39 and cysteine 515
Cysteine 497 and cysteine 515
Cysteine 108 and cysteine 121
A redox-regulated disulphide may form between cysteine 194 of Complement component C8 alpha chain and cysteine 60 of Complement component C8 gamma chain (164 and 40 respectively in this structure).

Details

Redox score ?
84
PDB code
2rd7
Structure name
human complement membrane attack proteins share a common fold with bacterial cytolysins
Structure deposition date
2007-09-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide A name
Complement component C8 alpha chain
Peptide B name
Complement component C8 gamma chain
Peptide A accession
P07357
Peptide B accession
P07360
Peptide A residue number
194
Peptide B residue number
60

Ligandability

Cysteine 194 of Complement component C8 alpha 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 60 of Complement component C8 gamma 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 alpha chain between cysteines 551 and 584 (521 and 554 respectively in this structure).

Details

Redox score ?
93
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
551
Residue number B
584
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 551 of Complement component C8 alpha 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 584 of Complement component C8 alpha 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 alpha chain between cysteines 562 and 574 (532 and 544 respectively in this structure).

Details

Redox score ?
91
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
P07357
Residue number A
562
Residue number B
574
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 562 of Complement component C8 alpha 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 574 of Complement component C8 alpha 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 alpha chain between cysteines 53 and 90 (23 and 60 respectively in this structure).

Details

Redox score ?
89
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
P07357
Residue number A
53
Residue number B
90
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 53 of Complement component C8 alpha 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 90 of Complement component C8 alpha 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 alpha chain between cysteines 39 and 74 (9 and 44 respectively in this structure).

Details

Redox score ?
88
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 ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
39
Residue number B
74
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 39 of Complement component C8 alpha 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 74 of Complement component C8 alpha 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 alpha chain between cysteines 50 and 84 (20 and 54 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
P07357
Residue number A
50
Residue number B
84
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 50 of Complement component C8 alpha 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 84 of Complement component C8 alpha 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 alpha chain between cysteines 502 and 517 (472 and 487 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 ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
502
Residue number B
517
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 502 of Complement component C8 alpha 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 517 of Complement component C8 alpha 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 alpha chain between cysteines 115 and 130 (85 and 100 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 ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
115
Residue number B
130
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 115 of Complement component C8 alpha 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 130 of Complement component C8 alpha 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 alpha chain between cysteines 519 and 528 (489 and 498 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 ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
519
Residue number B
528
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 519 of Complement component C8 alpha 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 528 of Complement component C8 alpha 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 alpha chain between cysteines 102 and 121 (72 and 91 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 ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
102
Residue number B
121
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 102 of Complement component C8 alpha 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 121 of Complement component C8 alpha 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 alpha chain between cysteines 499 and 515 (469 and 485 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 ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
499
Residue number B
515
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 499 of Complement component C8 alpha 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 515 of Complement component C8 alpha 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 alpha chain between cysteines 96 and 108 (66 and 78 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 ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
96
Residue number B
108
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 96 of Complement component C8 alpha 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 108 of Complement component C8 alpha 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 alpha chain between cysteines 375 and 399 (345 and 369 respectively in this structure).

Details

Redox score ?
84
PDB code
2rd7
Structure name
human complement membrane attack proteins share a common fold with bacterial cytolysins
Structure deposition date
2007-09-21
Thiol separation (Å)
3
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
21
Peptide accession
P07357
Residue number A
375
Residue number B
399
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 375 of Complement component C8 alpha 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 399 of Complement component C8 alpha 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 alpha chain between cysteines 140 and 177 (110 and 147 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 ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
140
Residue number B
177
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 140 of Complement component C8 alpha 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 177 of Complement component C8 alpha 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 alpha chain between cysteines 497 and 544 (467 and 514 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 ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
497
Residue number B
544
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 497 of Complement component C8 alpha 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 544 of Complement component C8 alpha 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 alpha chain between cysteines 517 and 519 (487 and 489 respectively in this structure).

Details

Redox score ?
69
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 ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
517
Residue number B
519
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 517 of Complement component C8 alpha 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 519 of Complement component C8 alpha 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 alpha chain between cysteines 502 and 519 (472 and 489 respectively in this structure).

Details

Redox score ?
68
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 ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
502
Residue number B
519
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 502 of Complement component C8 alpha 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 519 of Complement component C8 alpha 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 alpha chain between cysteines 502 and 528 (472 and 498 respectively in this structure).

Details

Redox score ?
61
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 ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
502
Residue number B
528
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 502 of Complement component C8 alpha 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 528 of Complement component C8 alpha 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 alpha chain between cysteines 517 and 528 (487 and 498 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)
7
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
517
Residue number B
528
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 517 of Complement component C8 alpha 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 528 of Complement component C8 alpha 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 alpha chain between cysteines 96 and 102 (66 and 72 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 ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
96
Residue number B
102
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 96 of Complement component C8 alpha 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 102 of Complement component C8 alpha 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 alpha chain between cysteines 499 and 517 (469 and 487 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
P07357
Residue number A
499
Residue number B
517
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 499 of Complement component C8 alpha 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 517 of Complement component C8 alpha 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 alpha chain between cysteines 515 and 517 (485 and 487 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
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 ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
515
Residue number B
517
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 515 of Complement component C8 alpha 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 517 of Complement component C8 alpha 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 alpha chain between cysteines 499 and 544 (469 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 ?
50
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 ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
499
Residue number B
544
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 499 of Complement component C8 alpha 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 544 of Complement component C8 alpha 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 alpha chain between cysteines 499 and 502 (469 and 472 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 ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
499
Residue number B
502
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 499 of Complement component C8 alpha 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 502 of Complement component C8 alpha 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 alpha chain between cysteines 96 and 121 (66 and 91 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)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
96
Residue number B
121
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 96 of Complement component C8 alpha 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 121 of Complement component C8 alpha 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 alpha chain between cysteines 497 and 499 (467 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 ?
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 ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
497
Residue number B
499
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 497 of Complement component C8 alpha 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 499 of Complement component C8 alpha 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 alpha chain between cysteines 102 and 108 (72 and 78 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 ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
102
Residue number B
108
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 102 of Complement component C8 alpha 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 108 of Complement component C8 alpha 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 alpha chain between cysteines 515 and 544 (485 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)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
515
Residue number B
544
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 515 of Complement component C8 alpha 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 544 of Complement component C8 alpha 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 alpha chain between cysteines 502 and 515 (472 and 485 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)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
502
Residue number B
515
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 502 of Complement component C8 alpha 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 515 of Complement component C8 alpha 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 alpha chain between cysteines 39 and 515 (9 and 485 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)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
39
Residue number B
515
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 39 of Complement component C8 alpha 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 515 of Complement component C8 alpha 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 alpha chain between cysteines 497 and 515 (467 and 485 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
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 ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
497
Residue number B
515
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 497 of Complement component C8 alpha 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 515 of Complement component C8 alpha 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 alpha chain between cysteines 108 and 121 (78 and 91 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
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 ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P07357
Residue number A
108
Residue number B
121
Peptide name
Complement component C8 alpha chain

Ligandability

Cysteine 108 of Complement component C8 alpha 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 121 of Complement component C8 alpha 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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