2QCM

Crystal structure of the orotidine-5'-monophosphate decarboxylase domain (Asp312Asn mutant) of human UMP synthase bound to 6-hydroxymethyl-UMP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004590	molecular_function	orotidine-5'-phosphate decarboxylase activity
A	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
A	0044205	biological_process	'de novo' UMP biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE JW5 A 482

Chain	Residue
A	SER257
A	MET371
A	SER372
A	ILE401
A	PRO417
A	GLN430
A	TYR432
A	GLY450
A	ARG451
A	HOH488
A	HOH494
A	ASP259
A	HOH530
A	LYS281
A	HIS283
A	ASN312
A	ASP317
A	ILE318
A	THR321
A	ASN341

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: For OMPdecase activity => ECO:0000269|PubMed:18184586

Chain	Residue	Details
A	ASN312
A	LYS314
A	ASP317

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCD

Chain	Residue	Details
A	SER257
A	ASP317
A	THR321

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCD, ECO:0007744|PDB:2QCH

Chain	Residue	Details
A	ASP259
A	SER372
A	GLN430
A	GLY450

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site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCL

Chain	Residue	Details
A	LYS281
A	LYS314

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