ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Serine hydroxymethyltransferase, cytosolic

Intermolecular
Cysteine 188 of H-2 class I histocompatibility antigen, D-B alpha chain and cysteine 92 L
Cysteine 125 of H-2 class I histocompatibility antigen, D-B alpha chain and cysteine 92
Cysteine 109 of IgG H chain and cysteine 135
Intramolecular
Cysteine 204 and cysteine 389
Cysteine 96 and cysteine 262
A redox-regulated disulphide may form between cysteine 188 of H-2 class I histocompatibility antigen, D-B alpha chain and cysteine 92 of Pre-glycoprotein polyprotein GP complex (164 and 1 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
5jwe
Structure name
crystal structure of h-2db in complex with the lcmv-derived gp92-101 peptide
Structure deposition date
2016-05-12
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide A name
H-2 class I histocompatibility antigen, D-B alpha chain
Peptide B name
Pre-glycoprotein polyprotein GP complex
Peptide A accession
P01899
Peptide B accession
P09991
Peptide A residue number
188
Peptide B residue number
92

Ligandability

Cysteine 188 of H-2 class I histocompatibility antigen, D-B alpha chain

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.

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 92 of Pre-glycoprotein polyprotein GP complex

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 between cysteine 125 of H-2 class I histocompatibility antigen, D-B alpha chain and cysteine 92 of Pre-glycoprotein polyprotein GP complex (101 and 1 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
5jwe
Structure name
crystal structure of h-2db in complex with the lcmv-derived gp92-101 peptide
Structure deposition date
2016-05-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide A name
H-2 class I histocompatibility antigen, D-B alpha chain
Peptide B name
Pre-glycoprotein polyprotein GP complex
Peptide A accession
P01899
Peptide B accession
P09991
Peptide A residue number
125
Peptide B residue number
92

Ligandability

Cysteine 125 of H-2 class I histocompatibility antigen, D-B alpha chain

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 92 of Pre-glycoprotein polyprotein GP complex

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 between cysteine 109 of IgG H chain and cysteine 135 of Pre-glycoprotein polyprotein GP complex. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
5w1k
Structure name
junv gp1 cr1-10 fab cr1-28 fab complex
Structure deposition date
2017-06-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide A name
IgG H chain
Peptide B name
Pre-glycoprotein polyprotein GP complex
Peptide A accession
S6B2B6
Peptide B accession
P26313
Peptide A residue number
109
Peptide B residue number
135

Ligandability

Cysteine 109 of IgG H chain

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 135 of Pre-glycoprotein polyprotein GP complex

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 109 in protein A could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Serine hydroxymethyltransferase, cytosolic between cysteines 204 and 389. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
6fl5
Structure name
structure of human shmt1-h135n-r137a-e168n mutant at 3
Structure deposition date
2018-01-25
Thiol separation (Å)
8
Half-sphere exposure sum ?
90
Minimum pKa ?
11
% buried
89
Peptide accession
P34896
Residue number A
204
Residue number B
389
Peptide name
Serine hydroxymethyltransferase, cytosolic

Ligandability

Cysteine 204 of Serine hydroxymethyltransferase, cytosolic

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 389 of Serine hydroxymethyltransferase, cytosolic

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 Serine hydroxymethyltransferase, cytosolic between cysteines 96 and 262. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
1bj4
Structure name
recombinant serine hydroxymethyltransferase (human)
Structure deposition date
1998-07-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
88
Peptide accession
P34896
Residue number A
96
Residue number B
262
Peptide name
Serine hydroxymethyltransferase, cytosolic

Ligandability

Cysteine 96 of Serine hydroxymethyltransferase, cytosolic

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 262 of Serine hydroxymethyltransferase, cytosolic

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.

If this tool was useful for finding a disulphide, please cite: