2ZLB

Crystal structure of APO form of rat catechol-O-methyltransferase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0006584	biological_process	catecholamine metabolic process
A	0008171	molecular_function	O-methyltransferase activity
A	0016206	molecular_function	catechol O-methyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A 300

Chain	Residue
A	TYR68
A	CYS69
A	GLY70
A	TYR71
A	SER72
A	ASP141
A	HOH304
A	HOH322
A	HOH359

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01019","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12237326","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01019","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	7
Details	Binding site: {}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1vid

Chain	Residue	Details
A	GLU199
A	LYS144

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 915

Chain	Residue	Details
A	ASP141	metal ligand
A	LYS144	proton shuttle (general acid/base)
A	ASP169	metal ligand
A	ASN170	metal ligand
A	GLU199	electrostatic stabiliser

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