ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Gamma-crystallin B

Intramolecular
Cysteine 19 and cysteine 79
Cysteine 19 and cysteine 23
Cysteine 23 and cysteine 79
Cysteine 79 and cysteine 80
Cysteine 33 and cysteine 79
A redox-regulated disulphide may form within Gamma-crystallin B between cysteines 19 and 79 (18 and 78 respectively in this structure).

Details

Redox score ?
76
PDB code
2jdg
Structure name
affilin based on human gamma-b crystallin
Structure deposition date
2007-01-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
7
% buried
60
Peptide accession
P07316
Residue number A
19
Residue number B
79
Peptide name
Gamma-crystallin B

Ligandability

Cysteine 19 of Gamma-crystallin B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 79 of Gamma-crystallin B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Gamma-crystallin B between cysteines 19 and 23 (18 and 22 respectively in this structure).

Details

Redox score ?
76
PDB code
2jdg
Structure name
affilin based on human gamma-b crystallin
Structure deposition date
2007-01-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
56
Minimum pKa ?
7
% buried
32
Peptide accession
P07316
Residue number A
19
Residue number B
23
Peptide name
Gamma-crystallin B

Ligandability

Cysteine 19 of Gamma-crystallin B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 23 of Gamma-crystallin B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Gamma-crystallin B between cysteines 23 and 79 (22 and 78 respectively in this structure).

Details

Redox score ?
63
PDB code
2jdg
Structure name
affilin based on human gamma-b crystallin
Structure deposition date
2007-01-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
48
Peptide accession
P07316
Residue number A
23
Residue number B
79
Peptide name
Gamma-crystallin B

Ligandability

Cysteine 23 of Gamma-crystallin B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 79 of Gamma-crystallin B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Gamma-crystallin B between cysteines 79 and 80 (78 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 ?
46
PDB code
2jdg
Structure name
affilin based on human gamma-b crystallin
Structure deposition date
2007-01-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
10
% buried
74
Peptide accession
P07316
Residue number A
79
Residue number B
80
Peptide name
Gamma-crystallin B

Ligandability

Cysteine 79 of Gamma-crystallin B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 80 of Gamma-crystallin B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 Gamma-crystallin B between cysteines 33 and 79 (32 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 ?
28
PDB code
1i5i
Structure name
the c18s mutant of bovine (gamma-b)-crystallin
Structure deposition date
2001-02-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
90
Peptide accession
P02526
Residue number A
33
Residue number B
79
Peptide name
Gamma-crystallin B

Ligandability

Cysteine 33 of Gamma-crystallin B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 79 of Gamma-crystallin B

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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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