ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Leucine carboxyl methyltransferase 1

Intermolecular
Cysteine 136 and cysteine 136
Cysteine 30 and cysteine 136 L
Intramolecular
Cysteine 316 and cysteine 318 L
Cysteine 90 and cysteine 92
Cysteine 258 and cysteine 316 L
Cysteine 30 and cysteine 36 L
Cysteine 199 and cysteine 250 L
Cysteine 258 and cysteine 318 L
Cysteine 199 and cysteine 258 L
Cysteine 199 and cysteine 316
A redox-regulated disulphide may form between two units of Leucine carboxyl methyltransferase 1 at cysteines 136 and 136. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
3iei
Structure name
crystal structure of human leucine carboxylmethyltransferase-1 in complex with s-adenosyl homocysteine
Structure deposition date
2009-07-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
100
Peptide A name
Leucine carboxyl methyltransferase 1
Peptide B name
Leucine carboxyl methyltransferase 1
Peptide A accession
Q9UIC8
Peptide B accession
Q9UIC8
Peptide A residue number
136
Peptide B residue number
136

Ligandability

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 two units of Leucine carboxyl methyltransferase 1 at cysteines 30 and 136. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
3iei
Structure name
crystal structure of human leucine carboxylmethyltransferase-1 in complex with s-adenosyl homocysteine
Structure deposition date
2009-07-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
11
% buried
100
Peptide A name
Leucine carboxyl methyltransferase 1
Peptide B name
Leucine carboxyl methyltransferase 1
Peptide A accession
Q9UIC8
Peptide B accession
Q9UIC8
Peptide A residue number
30
Peptide B residue number
136

Ligandability

Cysteine 30 of Leucine carboxyl methyltransferase 1

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 136 of Leucine carboxyl methyltransferase 1

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 Leucine carboxyl methyltransferase 1 between cysteines 316 and 318.

Details

Redox score ?
68
PDB code
3iei
Structure name
crystal structure of human leucine carboxylmethyltransferase-1 in complex with s-adenosyl homocysteine
Structure deposition date
2009-07-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
89
Minimum pKa ?
9
% buried
100
Peptide accession
Q9UIC8
Residue number A
316
Residue number B
318
Peptide name
Leucine carboxyl methyltransferase 1

Ligandability

Cysteine 316 of Leucine carboxyl methyltransferase 1

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 318 of Leucine carboxyl methyltransferase 1

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 Leucine carboxyl methyltransferase 1 between cysteines 90 and 92.

Details

Redox score ?
62
PDB code
3iei
Structure name
crystal structure of human leucine carboxylmethyltransferase-1 in complex with s-adenosyl homocysteine
Structure deposition date
2009-07-22
Thiol separation (Å)
6
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
54
Peptide accession
Q9UIC8
Residue number A
90
Residue number B
92
Peptide name
Leucine carboxyl methyltransferase 1

Ligandability

Cysteine 90 of Leucine carboxyl methyltransferase 1

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 Leucine carboxyl methyltransferase 1

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 Leucine carboxyl methyltransferase 1 between cysteines 258 and 316. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
3iei
Structure name
crystal structure of human leucine carboxylmethyltransferase-1 in complex with s-adenosyl homocysteine
Structure deposition date
2009-07-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
83
Minimum pKa ?
14
% buried
96
Peptide accession
Q9UIC8
Residue number A
258
Residue number B
316
Peptide name
Leucine carboxyl methyltransferase 1

Ligandability

Cysteine 258 of Leucine carboxyl methyltransferase 1

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.

Cysteine 316 of Leucine carboxyl methyltransferase 1

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 Leucine carboxyl methyltransferase 1 between cysteines 30 and 36. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
3o7w
Structure name
the crystal structure of human leucine carboxyl methyltransferase 1
Structure deposition date
2010-08-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
43
Minimum pKa ?
9
% buried
27
Peptide accession
Q9UIC8
Residue number A
30
Residue number B
36
Peptide name
Leucine carboxyl methyltransferase 1

Ligandability

Cysteine 30 of Leucine carboxyl methyltransferase 1

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 36 of Leucine carboxyl methyltransferase 1

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 Leucine carboxyl methyltransferase 1 between cysteines 199 and 250. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
3iei
Structure name
crystal structure of human leucine carboxylmethyltransferase-1 in complex with s-adenosyl homocysteine
Structure deposition date
2009-07-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
11
% buried
75
Peptide accession
Q9UIC8
Residue number A
199
Residue number B
250
Peptide name
Leucine carboxyl methyltransferase 1

Ligandability

Cysteine 199 of Leucine carboxyl methyltransferase 1

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 250 of Leucine carboxyl methyltransferase 1

Not ligandable in the dataset of Yang et al.

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 Leucine carboxyl methyltransferase 1 between cysteines 258 and 318. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
3iei
Structure name
crystal structure of human leucine carboxylmethyltransferase-1 in complex with s-adenosyl homocysteine
Structure deposition date
2009-07-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
9
% buried
96
Peptide accession
Q9UIC8
Residue number A
258
Residue number B
318
Peptide name
Leucine carboxyl methyltransferase 1

Ligandability

Cysteine 258 of Leucine carboxyl methyltransferase 1

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.

Cysteine 318 of Leucine carboxyl methyltransferase 1

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 Leucine carboxyl methyltransferase 1 between cysteines 199 and 258. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
3iei
Structure name
crystal structure of human leucine carboxylmethyltransferase-1 in complex with s-adenosyl homocysteine
Structure deposition date
2009-07-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
97
Peptide accession
Q9UIC8
Residue number A
199
Residue number B
258
Peptide name
Leucine carboxyl methyltransferase 1

Ligandability

Cysteine 199 of Leucine carboxyl methyltransferase 1

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 258 of Leucine carboxyl methyltransferase 1

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 Leucine carboxyl methyltransferase 1 between cysteines 199 and 316. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
3iei
Structure name
crystal structure of human leucine carboxylmethyltransferase-1 in complex with s-adenosyl homocysteine
Structure deposition date
2009-07-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
11
% buried
100
Peptide accession
Q9UIC8
Residue number A
199
Residue number B
316
Peptide name
Leucine carboxyl methyltransferase 1

Ligandability

Cysteine 199 of Leucine carboxyl methyltransferase 1

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 316 of Leucine carboxyl methyltransferase 1

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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