Structure of PDB 2qcd Chain A

Receptor sequence
>2qcdA (length=258) Species: 9606 (Homo sapiens) [Search protein sequence]
AMELSFGARAELPRIHPVASKLLRLMQKKETNLCLSADVSLARELLQLAD
ALGPSICMLKTHVDILNDFTLDVMKELITLAKCHEFLIFEDRKFADIGNT
VKKQYEGGIFKIASWADLVNAHVVPGSGVVKGLQEVGLPLHRGCLLIAEM
SSTGSLATGDYTRAAVRMAEEHSEFVVGFISGSRVSMKPEFLHLTPGVQL
EAGGDNLGQQYNSPQEVIGKRGSDIIIVGRGIISAADRLEAAEMYRKAAW
EAYLSRLG
3D structure
PDB2qcd Structures of the human orotidine-5'-monophosphate decarboxylase support a covalent mechanism and provide a framework for drug design.
ChainA
Resolution2.03 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.4.2.10: orotate phosphoribosyltransferase.
4.1.1.23: orotidine-5'-phosphate decarboxylase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 U5P A S257 D259 K281 H283 K314 M371 S372 P417 Q430 Y432 G450 R451 S36 D38 K60 H62 K93 M150 S151 P196 Q209 Y211 G229 R230 PDBbind-CN: -logKd/Ki=3.40,IC50=400uM
BS02 U5P A D317 I318 T321 D96 I97 T100 PDBbind-CN: -logKd/Ki=3.40,IC50=400uM
Gene Ontology
Molecular Function
GO:0004590 orotidine-5'-phosphate decarboxylase activity
Biological Process
GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process
GO:0044205 'de novo' UMP biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2qcd, PDBe:2qcd, PDBj:2qcd
PDBsum2qcd
PubMed18184586
UniProtP11172|UMPS_HUMAN Uridine 5'-monophosphate synthase (Gene Name=UMPS)

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