ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Retinol-binding protein 2

Intramolecular
Cysteine 122 and cysteine 127
Cysteine 96 and cysteine 122
Cysteine 96 and cysteine 32
A redox-regulated disulphide may form within Retinol-binding protein 2 between cysteines 122 and 127. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
1b4m
Structure name
nmr structure of apo cellular retinol-binding protein ii, 24 structures
Structure deposition date
1998-12-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
51
Peptide accession
P06768
Residue number A
122
Residue number B
127
Peptide name
Retinol-binding protein 2

Ligandability

Cysteine 122 of Retinol-binding protein 2

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 Retinol-binding protein 2

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 Retinol-binding protein 2 between cysteines 96 and 122. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
1eii
Structure name
nmr structure of holo cellular retinol-binding protein ii
Structure deposition date
2000-02-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
82
Peptide accession
P06768
Residue number A
96
Residue number B
122
Peptide name
Retinol-binding protein 2

Ligandability

Cysteine 96 of Retinol-binding protein 2

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 122 of Retinol-binding protein 2

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 Retinol-binding protein 2 between cysteines 96 and 32 (28 and 32 respectively in this structure).

Details

Redox score ?
nan
PDB code
6wnj
Structure name
the crystal structure of apo domain-swapped trimer q108k:t51d:a28c:i32c of hcrbpii
Structure deposition date
2020-04-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
nan
Peptide accession
P50120
Residue number A
96
Residue number B
32
Peptide name
Retinol-binding protein 2

Ligandability

Cysteine 96 of Retinol-binding protein 2

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 32 of Retinol-binding protein 2

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 28 has been assigned to correct residue.
Cysteine 32 in protein B could not be asigned to a Uniprot residue.
If this tool was useful for finding a disulphide, please cite: