S-adenosylmethionine decarboxylase proenzyme

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of S-adenosylmethionine decarboxylase proenzyme at cysteines 148 and 148 (148 and 1148 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

1i7m

Structure name

human s-adenosylmethionine decarboxylase with covalently bound pyruvoyl group and complexed with 4-amidinoindan-1-one-2'- amidinohydrazone

Structure deposition date

2001-03-09

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

% buried

100

Peptide A name

S-adenosylmethionine decarboxylase proenzyme

Peptide B name

S-adenosylmethionine decarboxylase proenzyme

Peptide A accession

P17707

Peptide B accession

P17707

Peptide A residue number

148

Peptide B residue number

148

Ligandability

Cysteine 148 of S-adenosylmethionine decarboxylase proenzyme

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 148 of S-adenosylmethionine decarboxylase proenzyme

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 S-adenosylmethionine decarboxylase proenzyme between cysteines 148 and 156.

Details

Redox score ?

PDB code

3h0v

Structure name

human adometdc with 5'-deoxy-5'-(dimethylsulfonio) adenosine

Structure deposition date

2009-04-10

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

P17707

Residue number A

148

Residue number B

156

Peptide name

S-adenosylmethionine decarboxylase proenzyme

Ligandability

Cysteine 148 of S-adenosylmethionine decarboxylase proenzyme

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 156 of S-adenosylmethionine decarboxylase proenzyme

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 S-adenosylmethionine decarboxylase proenzyme between cysteines 49 and 82. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?