ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Peptidoglycan recognition protein 3

Intramolecular
Cysteine 178 and cysteine 300
Cysteine 194 and cysteine 238
Cysteine 214 and cysteine 220
A redox-regulated disulphide may form within Peptidoglycan recognition protein 3 between cysteines 178 and 300.

Details

Redox score ?
86
PDB code
1sk3
Structure name
crystal structure of the c-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein ialpha
Structure deposition date
2004-03-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96LB9
Residue number A
178
Residue number B
300
Peptide name
Peptidoglycan recognition protein 3

Ligandability

Cysteine 178 of Peptidoglycan recognition protein 3

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 300 of Peptidoglycan recognition protein 3

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 Peptidoglycan recognition protein 3 between cysteines 194 and 238.

Details

Redox score ?
85
PDB code
1sk4
Structure name
crystal structure of the c-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein ialpha
Structure deposition date
2004-03-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96LB9
Residue number A
194
Residue number B
238
Peptide name
Peptidoglycan recognition protein 3

Ligandability

Cysteine 194 of Peptidoglycan recognition protein 3

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 238 of Peptidoglycan recognition protein 3

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 Peptidoglycan recognition protein 3 between cysteines 214 and 220.

Details

Redox score ?
84
PDB code
1twq
Structure name
crystal structure of the c-terminal pgn-binding domain of human pgrp- ialpha in complex with pgn analog muramyl tripeptide
Structure deposition date
2004-07-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96LB9
Residue number A
214
Residue number B
220
Peptide name
Peptidoglycan recognition protein 3

Ligandability

Cysteine 214 of Peptidoglycan recognition protein 3

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 220 of Peptidoglycan recognition protein 3

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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