ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Methionine synthase

Intramolecular
Cysteine 260 and cysteine 323
Cysteine 432 and cysteine 462
Cysteine 432 and cysteine 467
Cysteine 447 and cysteine 467
Cysteine 462 and cysteine 467
Cysteine 255 and cysteine 284
A redox-regulated disulphide may form within Methionine synthase between cysteines 260 and 323.

Details

Redox score ?
79
PDB code
4ccz
Structure name
crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
Structure deposition date
2013-10-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99707
Residue number A
260
Residue number B
323
Peptide name
Methionine synthase

Ligandability

Cysteine 260 of Methionine synthase

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 323 of Methionine synthase

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 synthase between cysteines 432 and 462. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
4ccz
Structure name
crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
Structure deposition date
2013-10-29
Thiol separation (Å)
6
Half-sphere exposure sum ?
95
Minimum pKa ?
11
% buried
94
Peptide accession
Q99707
Residue number A
432
Residue number B
462
Peptide name
Methionine synthase

Ligandability

Cysteine 432 of Methionine synthase

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 462 of Methionine synthase

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 synthase between cysteines 432 and 467. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
4ccz
Structure name
crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
Structure deposition date
2013-10-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
98
Minimum pKa ?
11
% buried
100
Peptide accession
Q99707
Residue number A
432
Residue number B
467
Peptide name
Methionine synthase

Ligandability

Cysteine 432 of Methionine synthase

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 467 of Methionine synthase

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 synthase between cysteines 447 and 467. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
4ccz
Structure name
crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
Structure deposition date
2013-10-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
95
Minimum pKa ?
11
% buried
100
Peptide accession
Q99707
Residue number A
447
Residue number B
467
Peptide name
Methionine synthase

Ligandability

Cysteine 447 of Methionine synthase

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 467 of Methionine synthase

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 synthase between cysteines 462 and 467. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
4ccz
Structure name
crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
Structure deposition date
2013-10-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
95
Minimum pKa ?
11
% buried
94
Peptide accession
Q99707
Residue number A
462
Residue number B
467
Peptide name
Methionine synthase

Ligandability

Cysteine 462 of Methionine synthase

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 467 of Methionine synthase

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 synthase between cysteines 255 and 284. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
4ccz
Structure name
crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
Structure deposition date
2013-10-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
89
Minimum pKa ?
11
% buried
92
Peptide accession
Q99707
Residue number A
255
Residue number B
284
Peptide name
Methionine synthase

Ligandability

Cysteine 255 of Methionine synthase

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 284 of Methionine synthase

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: