Catechol O-methyltransferase

Intramolecular

A redox-regulated disulphide may form within Catechol O-methyltransferase between cysteines 112 and 95 (69 and 95 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

5k09

Structure name

crystal structure of comt in complex with a thiazole ligand

Structure deposition date

2016-05-17

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide accession

P22734

Residue number A

112

Residue number B

Peptide name

Catechol O-methyltransferase

Ligandability

Cysteine 112 of Catechol O-methyltransferase

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 95 of Catechol O-methyltransferase

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 95 in protein B could not be asigned to a Uniprot residue.

A redox-regulated disulphide may form within Catechol O-methyltransferase between cysteines 83 and 119 (33 and 69 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?