5K01

Crystal Structure of COMT in complex with 2,7-dimethyl-3-(1H-pyrazol-3-yl)imidazo[1,2-a]pyridine

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	12
Details	binding site for residue 6OW A 301

Chain	Residue
A	ARG55
A	GLN120
A	HIS142
A	TRP143
A	GLU56
A	GLY66
A	TYR68
A	MET89
A	GLU90
A	ILE91
A	ALA118
A	SER119

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site_id	AC2
Number of Residues	6
Details	binding site for residue K A 302

Chain	Residue
A	VAL183
A	ARG184
A	SER186
A	PHE189
A	HOH552
A	HOH574

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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	ILE91
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	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903

Chain	Residue	Details
A	SER216

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Catalytic Information from CSA

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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