3MO7

Crystal structure of human orotidine 5'-monophosphate decarboxylase covalently modified by 2'-fluoro-6-iodo-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 UFT A 3000

Chain	Residue
A	HOH3
A	ASP128
A	ILE129
A	THR132
A	MET182
A	SER183
A	PRO228
A	GLN241
A	TYR243
A	GLY261
A	ARG262
A	HOH4
A	HOH295
A	HOH5
A	SER68
A	ASP70
A	LYS92
A	HIS94
A	ASP123
A	LYS125

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 1000

Chain	Residue
A	LYS53
A	ALA113
A	PHE118
A	LEU119
A	ASP149
A	HOH359
A	HOH402

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Functional Information from PROSITE/UniProt

site_id	PS00156
Number of Residues	14
Details	OMPDECASE Orotidine 5'-phosphate decarboxylase active site. IFeDrKfaDIGnTV

Chain	Residue	Details
A	ILE120-VAL133

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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	ASP123
A	LYS125
A	ASP128

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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	SER68
A	ASP128
A	THR132

---

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	ASP70
A	SER183
A	GLN241
A	GLY261

---

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

Chain	Residue	Details
A	LYS92
A	LYS125

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