Structure of PDB 1loq Chain A

Receptor sequence
>1loqA (length=209) Species: 2157 (Archaea) [Search protein sequence]
RLILAMDLMNRDDALRVTGEVREYIDTVKIGYPLVLSEGMDIIAEFRKRF
GCRIIADFKVADIPETNEKICRATFKAGADAIIVHGFPGADSVRACLNVA
EEMGREVFLLTEMSHPGAEMFIQGAADEIARMGVDLGVKNYVGPSTRPER
LSRLREIIGQDSFLISPGVGAQGGDPGETLRFADAIIVGRSIYLADNPAA
AAAGIIESI
3D structure
PDB1loq Crystal structures of inhibitor complexes reveal an alternate binding mode in orotidine-5'-monophosphate decarboxylase.
ChainA
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K42 D70 K72 D75
Catalytic site (residue number reindexed from 1) K29 D57 K59 D62
Enzyme Commision number 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 U A D20 K42 D70 K72 M126 S127 P180 Q185 G202 R203 D7 K29 D57 K59 M113 S114 P167 Q172 G189 R190 MOAD: Ki=0.2mM
PDBbind-CN: -logKd/Ki=3.70,Ki=0.2mM
Gene Ontology
Molecular Function
GO:0004590 orotidine-5'-phosphate decarboxylase activity
GO:0016831 carboxy-lyase activity
Biological Process
GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process
GO:0006221 pyrimidine nucleotide biosynthetic process
GO:0044205 'de novo' UMP biosynthetic process
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:1loq, PDBe:1loq, PDBj:1loq
PDBsum1loq
PubMed12011084
UniProtO26232|PYRF_METTH Orotidine 5'-phosphate decarboxylase (Gene Name=pyrF)

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