ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Methionine aminopeptidase 2

Intramolecular
Cysteine 228 and cysteine 448 L
Cysteine 197 and cysteine 223
Cysteine 380 and cysteine 436 L
Cysteine 223 and cysteine 248
Cysteine 197 and cysteine 416
Cysteine 197 and cysteine 248
Cysteine 135 and cysteine 468
Cysteine 290 and cysteine 298
Cysteine 223 and cysteine 228
Cysteine 228 and cysteine 248
Cysteine 223 and cysteine 416
A redox-regulated disulphide may form within Methionine aminopeptidase 2 between cysteines 228 and 448.

Details

Redox score ?
72
PDB code
1b6a
Structure name
human methionine aminopeptidase 2 complexed with tnp-470
Structure deposition date
1999-01-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
79
Minimum pKa ?
7
% buried
79
Peptide accession
P50579
Residue number A
228
Residue number B
448
Peptide name
Methionine aminopeptidase 2

Ligandability

Cysteine 228 of Methionine aminopeptidase 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 448 of Methionine aminopeptidase 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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Methionine aminopeptidase 2 between cysteines 197 and 223.

Details

Redox score ?
70
PDB code
6qeg
Structure name
crystal structure of human methionine aminopeptidase-2 in complex with an inhibitor 2-oxo-1-phenyl-pyrrolidine-3-carboxylic acid (2- thiophen-2-yl-ethyl)-amide
Structure deposition date
2019-01-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
85
Minimum pKa ?
8
% buried
100
Peptide accession
P50579
Residue number A
197
Residue number B
223
Peptide name
Methionine aminopeptidase 2

Ligandability

Cysteine 197 of Methionine aminopeptidase 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 223 of Methionine aminopeptidase 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 Methionine aminopeptidase 2 between cysteines 380 and 436. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
7a14
Structure name
crystal structure of human methionine aminopeptidase-2 in complex with an inhibitor gsk2218325a (compound 32)
Structure deposition date
2020-08-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
53
Minimum pKa ?
11
% buried
60
Peptide accession
P50579
Residue number A
380
Residue number B
436
Peptide name
Methionine aminopeptidase 2

Ligandability

Cysteine 380 of Methionine aminopeptidase 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 436 of Methionine aminopeptidase 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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Methionine aminopeptidase 2 between cysteines 223 and 248. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2ga2
Structure name
h-metap2 complexed with a193400
Structure deposition date
2006-03-07
Thiol separation (Å)
5
Half-sphere exposure sum ?
88
Minimum pKa ?
13
% buried
100
Peptide accession
P50579
Residue number A
223
Residue number B
248
Peptide name
Methionine aminopeptidase 2

Ligandability

Cysteine 223 of Methionine aminopeptidase 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 248 of Methionine aminopeptidase 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 Methionine aminopeptidase 2 between cysteines 197 and 416. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
2oaz
Structure name
human methionine aminopeptidase-2 complexed with sb-587094
Structure deposition date
2006-12-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
81
Minimum pKa ?
8
% buried
100
Peptide accession
P50579
Residue number A
197
Residue number B
416
Peptide name
Methionine aminopeptidase 2

Ligandability

Cysteine 197 of Methionine aminopeptidase 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 416 of Methionine aminopeptidase 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 Methionine aminopeptidase 2 between cysteines 197 and 248. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
5lyw
Structure name
crystal structure of human methionine aminopeptidase-2 in complex; with an inhibitor 6-((r)-2-o-tolyloxymethyl-pyrrolidin-1-yl)-9h- purine
Structure deposition date
2016-09-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
81
Minimum pKa ?
8
% buried
100
Peptide accession
P50579
Residue number A
197
Residue number B
248
Peptide name
Methionine aminopeptidase 2

Ligandability

Cysteine 197 of Methionine aminopeptidase 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 248 of Methionine aminopeptidase 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 Methionine aminopeptidase 2 between cysteines 135 and 468. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
2ea4
Structure name
h-metap2 complexed with a797859
Structure deposition date
2007-01-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
54
Peptide accession
P50579
Residue number A
135
Residue number B
468
Peptide name
Methionine aminopeptidase 2

Ligandability

Cysteine 135 of Methionine aminopeptidase 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 468 of Methionine aminopeptidase 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 Methionine aminopeptidase 2 between cysteines 290 and 298. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
2ga2
Structure name
h-metap2 complexed with a193400
Structure deposition date
2006-03-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
34
Peptide accession
P50579
Residue number A
290
Residue number B
298
Peptide name
Methionine aminopeptidase 2

Ligandability

Cysteine 290 of Methionine aminopeptidase 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 298 of Methionine aminopeptidase 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 Methionine aminopeptidase 2 between cysteines 223 and 228. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
6qej
Structure name
crystal structure of human methionine aminopeptidase-2 in complex with an inhibitor thiophene-2-sulfonic acid (4-fluoro-benzyl)-(4h-[1,2, 4]triazol-3-ylmethyl)-amide
Structure deposition date
2019-01-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
89
Minimum pKa ?
8
% buried
92
Peptide accession
P50579
Residue number A
223
Residue number B
228
Peptide name
Methionine aminopeptidase 2

Ligandability

Cysteine 223 of Methionine aminopeptidase 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 228 of Methionine aminopeptidase 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 Methionine aminopeptidase 2 between cysteines 228 and 248. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
6qef
Structure name
crystal structure of human methionine aminopeptidase-2 in complex with an inhibitor (s)-3-hydroxy-2-oxo-1-phenyl-pyrrolidine-3-carboxylic acid 3-chloro-5-fluoro-benzylamide
Structure deposition date
2019-01-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
87
Minimum pKa ?
7
% buried
100
Peptide accession
P50579
Residue number A
228
Residue number B
248
Peptide name
Methionine aminopeptidase 2

Ligandability

Cysteine 228 of Methionine aminopeptidase 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 248 of Methionine aminopeptidase 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 Methionine aminopeptidase 2 between cysteines 223 and 416. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
PDB code
2oaz
Structure name
human methionine aminopeptidase-2 complexed with sb-587094
Structure deposition date
2006-12-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
87
Minimum pKa ?
12
% buried
100
Peptide accession
P50579
Residue number A
223
Residue number B
416
Peptide name
Methionine aminopeptidase 2

Ligandability

Cysteine 223 of Methionine aminopeptidase 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 416 of Methionine aminopeptidase 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.

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