ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Gamma-crystallin D

Intramolecular
Cysteine 19 and cysteine 79
Cysteine 109 and cysteine 111
Cysteine 19 and cysteine 33
Cysteine 33 and cysteine 79
Cysteine 42 and cysteine 79
A redox-regulated disulphide may form within Gamma-crystallin D between cysteines 19 and 79 (18 and 78 respectively in this structure).

Details

Redox score ?
75
PDB code
1hk0
Structure name
human gammad crystallin structure at 1
Structure deposition date
2003-03-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
8
% buried
73
Peptide accession
P07320
Residue number A
19
Residue number B
79
Peptide name
Gamma-crystallin D

Ligandability

Cysteine 19 of Gamma-crystallin D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 D between cysteines 109 and 111 (108 and 110 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
4jgf
Structure name
crystal structure of the cataract-causing p23t gamma d-crystallin mutant
Structure deposition date
2013-03-01
Thiol separation (Å)
6
Half-sphere exposure sum ?
51
Minimum pKa ?
10
% buried
16
Peptide accession
P07320
Residue number A
109
Residue number B
111
Peptide name
Gamma-crystallin D

Ligandability

Cysteine 109 of Gamma-crystallin D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 111 of Gamma-crystallin D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 D between cysteines 19 and 33 (18 and 32 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
7p53
Structure name
crystal structure of human gamma-d-crystallin mutant c110m at 1
Structure deposition date
2021-07-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
8
% buried
81
Peptide accession
P07320
Residue number A
19
Residue number B
33
Peptide name
Gamma-crystallin D

Ligandability

Cysteine 19 of Gamma-crystallin D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 33 of Gamma-crystallin D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 D 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 ?
33
PDB code
1hk0
Structure name
human gammad crystallin structure at 1
Structure deposition date
2003-03-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
12
% buried
94
Peptide accession
P07320
Residue number A
33
Residue number B
79
Peptide name
Gamma-crystallin D

Ligandability

Cysteine 33 of Gamma-crystallin D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 D between cysteines 42 and 79. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
2klj
Structure name
solution structure of gammad-crystallin with rdc and saxs
Structure deposition date
2009-07-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
12
% buried
90
Peptide accession
P07320
Residue number A
42
Residue number B
79
Peptide name
Gamma-crystallin D

Ligandability

Cysteine 42 of Gamma-crystallin D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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 D

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in 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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