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: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019, ECO:0000269|PubMed:12237326

Chain	Residue	Details
A	VAL42
A	SER72
A	GLU90
A	ASP141

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019

Chain	Residue	Details
A	GLU64
A	MET91
A	SER119

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site_id	SWS_FT_FI3
Number of Residues	5
Details	BINDING:

Chain	Residue	Details
A	GLY117
A	LYS144
A	ASP169
A	ASN170
A	GLU199

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site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903

Chain	Residue	Details
A	SER216
A	SER217
A	SER221

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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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