Structure of PDB 6yvl Chain A

Receptor sequence
>6yvlA (length=256) Species: 9606 (Homo sapiens) [Search protein sequence]
ELSFGARAELPRIHPVASKLLRLMQKKETNLCLSADVSLARELLQLADAL
GPSICMLKTHVDILNDFTLDVMKELITLAKCHEFLIFEDRKFADIGNTVK
KQYEGGIFKIASWADLVNAHVVPGSGVVKGLQEVGLPLHRGCLLIAEMSS
TGSLATGDYTRAAVRMAEEHSEFVVGFISGSRVSMKPEFLHLTPGVQLEA
GGDNLGQQYNSPQEVIGKRGSDIIIVGRGIISAADRLEAAEMYRKAAWEA
YLSRLG
3D structure
PDB6yvl Ground-state destabilization by electrostatic repulsion is not a driving force in orotidine-5-monophosphate decarboxylase catalysis
ChainA
Resolution1.25 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 OMP A S257 D259 K281 H283 D312 K314 M371 S372 P417 Q430 Y432 G450 R451 S34 D36 K58 H60 D89 K91 M148 S149 P194 Q207 Y209 G227 R228
BS02 U A S257 D259 K281 H283 K314 M371 S372 P417 Q430 Y432 G450 R451 S34 D36 K58 H60 K91 M148 S149 P194 Q207 Y209 G227 R228
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:6yvl, PDBe:6yvl, PDBj:6yvl
PDBsum6yvl
PubMed
UniProtP11172|UMPS_HUMAN Uridine 5'-monophosphate synthase (Gene Name=UMPS)

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