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a tool for identifying drug-targetable redox-active disulphides

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Complement component C9

Intramolecular
Cysteine 380 and cysteine 119
Cysteine 513 and cysteine 528
Cysteine 530 and cysteine 539
Cysteine 57 and cysteine 94
Cysteine 119 and cysteine 134
Cysteine 101 and cysteine 112
Cysteine 510 and cysteine 526
Cysteine 107 and cysteine 125
Cysteine 43 and cysteine 78
Cysteine 54 and cysteine 88
More...
Cysteine 142 and cysteine 181
Cysteine 513 and cysteine 539
Cysteine 528 and cysteine 539
Cysteine 380 and cysteine 405
Cysteine 513 and cysteine 530
Cysteine 528 and cysteine 530
Cysteine 101 and cysteine 107
Cysteine 510 and cysteine 513
Cysteine 78 and cysteine 510
Cysteine 513 and cysteine 526
Cysteine 510 and cysteine 528
Cysteine 43 and cysteine 510
Cysteine 107 and cysteine 112
Cysteine 101 and cysteine 125
Cysteine 41 and cysteine 529
Cysteine 526 and cysteine 528
Cysteine 112 and cysteine 125
Cysteine 78 and cysteine 526
A redox-regulated disulphide may form within Complement component C9 between cysteines 380 and 119 (359 and 384 respectively in this structure).

Details

Redox score ?
89
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
P02748
Residue number A
380
Residue number B
119
Peptide name
Complement component C9

Ligandability

Cysteine 380 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 119 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Uncertain whether structure cysteine 384 has been assigned to correct residue.
A redox-regulated disulphide may form within Complement component C9 between cysteines 513 and 528 (492 and 507 respectively in this structure).

Details

Redox score ?
88
PDB code
6dlw
Structure name
complement component polyc9
Structure deposition date
2018-06-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02748
Residue number A
513
Residue number B
528
Peptide name
Complement component C9

Ligandability

Cysteine 513 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 530 and 539 (509 and 518 respectively in this structure).

Details

Redox score ?
88
PDB code
6h04
Structure name
closed conformation of the membrane attack complex
Structure deposition date
2018-07-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02748
Residue number A
530
Residue number B
539
Peptide name
Complement component C9

Ligandability

Cysteine 530 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 539 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 57 and 94 (36 and 73 respectively in this structure).

Details

Redox score ?
87
PDB code
6h04
Structure name
closed conformation of the membrane attack complex
Structure deposition date
2018-07-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
38
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02748
Residue number A
57
Residue number B
94
Peptide name
Complement component C9

Ligandability

Cysteine 57 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 94 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 119 and 134 (98 and 113 respectively in this structure).

Details

Redox score ?
86
PDB code
6dlw
Structure name
complement component polyc9
Structure deposition date
2018-06-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
41
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02748
Residue number A
119
Residue number B
134
Peptide name
Complement component C9

Ligandability

Cysteine 119 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 134 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 101 and 112 (80 and 91 respectively in this structure).

Details

Redox score ?
86
PDB code
6dlw
Structure name
complement component polyc9
Structure deposition date
2018-06-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02748
Residue number A
101
Residue number B
112
Peptide name
Complement component C9

Ligandability

Cysteine 101 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 112 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 510 and 526 (489 and 505 respectively in this structure).

Details

Redox score ?
86
PDB code
6dlw
Structure name
complement component polyc9
Structure deposition date
2018-06-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02748
Residue number A
510
Residue number B
526
Peptide name
Complement component C9

Ligandability

Cysteine 510 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 526 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 107 and 125 (86 and 104 respectively in this structure).

Details

Redox score ?
85
PDB code
6dlw
Structure name
complement component polyc9
Structure deposition date
2018-06-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02748
Residue number A
107
Residue number B
125
Peptide name
Complement component C9

Ligandability

Cysteine 107 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 125 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 43 and 78 (22 and 57 respectively in this structure).

Details

Redox score ?
85
PDB code
6dlw
Structure name
complement component polyc9
Structure deposition date
2018-06-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02748
Residue number A
43
Residue number B
78
Peptide name
Complement component C9

Ligandability

Cysteine 43 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 78 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 54 and 88 (33 and 67 respectively in this structure).

Details

Redox score ?
85
PDB code
6h04
Structure name
closed conformation of the membrane attack complex
Structure deposition date
2018-07-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02748
Residue number A
54
Residue number B
88
Peptide name
Complement component C9

Ligandability

Cysteine 54 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 88 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 142 and 181 (121 and 160 respectively in this structure).

Details

Redox score ?
83
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02748
Residue number A
142
Residue number B
181
Peptide name
Complement component C9

Ligandability

Cysteine 142 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 513 and 539 (492 and 518 respectively in this structure).

Details

Redox score ?
77
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02748
Residue number A
513
Residue number B
539
Peptide name
Complement component C9

Ligandability

Cysteine 513 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 539 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 528 and 539 (507 and 518 respectively in this structure).

Details

Redox score ?
75
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02748
Residue number A
528
Residue number B
539
Peptide name
Complement component C9

Ligandability

Cysteine 528 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 539 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 380 and 405 (359 and 384 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 ?
59
Minimum pKa ?
10
% buried
37
Peptide accession
P02748
Residue number A
380
Residue number B
405
Peptide name
Complement component C9

Ligandability

Cysteine 380 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 405 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 513 and 530 (492 and 509 respectively in this structure).

Details

Redox score ?
61
PDB code
6dlw
Structure name
complement component polyc9
Structure deposition date
2018-06-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02748
Residue number A
513
Residue number B
530
Peptide name
Complement component C9

Ligandability

Cysteine 513 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 530 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 528 and 530 (507 and 509 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
6dlw
Structure name
complement component polyc9
Structure deposition date
2018-06-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02748
Residue number A
528
Residue number B
530
Peptide name
Complement component C9

Ligandability

Cysteine 528 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 530 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 101 and 107 (80 and 86 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02748
Residue number A
101
Residue number B
107
Peptide name
Complement component C9

Ligandability

Cysteine 101 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 107 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 510 and 513 (489 and 492 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
6dlw
Structure name
complement component polyc9
Structure deposition date
2018-06-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02748
Residue number A
510
Residue number B
513
Peptide name
Complement component C9

Ligandability

Cysteine 510 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 513 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 78 and 510 (57 and 489 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
6dlw
Structure name
complement component polyc9
Structure deposition date
2018-06-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02748
Residue number A
78
Residue number B
510
Peptide name
Complement component C9

Ligandability

Cysteine 78 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 510 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 513 and 526 (492 and 505 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
6dlw
Structure name
complement component polyc9
Structure deposition date
2018-06-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02748
Residue number A
513
Residue number B
526
Peptide name
Complement component C9

Ligandability

Cysteine 513 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 526 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 510 and 528 (489 and 507 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
6h04
Structure name
closed conformation of the membrane attack complex
Structure deposition date
2018-07-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02748
Residue number A
510
Residue number B
528
Peptide name
Complement component C9

Ligandability

Cysteine 510 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 43 and 510 (22 and 489 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
6dlw
Structure name
complement component polyc9
Structure deposition date
2018-06-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02748
Residue number A
43
Residue number B
510
Peptide name
Complement component C9

Ligandability

Cysteine 43 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 510 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 107 and 112 (86 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 ?
46
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02748
Residue number A
107
Residue number B
112
Peptide name
Complement component C9

Ligandability

Cysteine 107 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 112 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 101 and 125 (80 and 104 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
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02748
Residue number A
101
Residue number B
125
Peptide name
Complement component C9

Ligandability

Cysteine 101 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 125 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 41 and 529 (21 and 509 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
6cxo
Structure name
complement component-9
Structure deposition date
2018-04-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P06683
Residue number A
41
Residue number B
529
Peptide name
Complement component C9

Ligandability

Cysteine 41 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 529 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 526 and 528 (505 and 507 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
P02748
Residue number A
526
Residue number B
528
Peptide name
Complement component C9

Ligandability

Cysteine 526 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 112 and 125 (91 and 104 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02748
Residue number A
112
Residue number B
125
Peptide name
Complement component C9

Ligandability

Cysteine 112 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 125 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 C9 between cysteines 78 and 526 (57 and 505 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
7nyc
Structure name
cryoem structure of 3c9-smac
Structure deposition date
2021-03-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P02748
Residue number A
78
Residue number B
526
Peptide name
Complement component C9

Ligandability

Cysteine 78 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 526 of Complement component C9

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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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