Structure of PDB 3wjw Chain A

Receptor sequence
>3wjwA (length=215) Species: 187420 (Methanothermobacter thermautotrophicus str. Delta H) [Search protein sequence]
VMNRLILAMDLMNRDDALRVTGEVREYIDTVKIGYPLVLSEGMDIIAEFR
KRFGCRIIADFKVADIPETNEKICRATFKAGADAIIVHGFPGADSVRACL
NVAEEMGREVFLLTEMSHPGAEMFIQGAADEIARMGVDLGVKNYVGPSTR
PERLSRLREIIGQDSFLISPGVGAQGGDPGETLRFADAIIVGRSIYLADN
PAAAAAGIIESIKDL
3D structure
PDB3wjw Substrate distortion contributes to the catalysis of orotidine 5'-monophosphate decarboxylase.
ChainA
Resolution1.59 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) K32 D60 K62 D65
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 U6M A D20 K42 D70 K72 M126 S127 P180 Q185 G202 R203 D10 K32 D60 K62 M116 S117 P170 Q175 G192 R193 MOAD: Ki=134uM
PDBbind-CN: -logKd/Ki=3.87,Ki=134uM
BindingDB: Ki=134000nM
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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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3wjw, PDBe:3wjw, PDBj:3wjw
PDBsum3wjw
PubMed24151964
UniProtO26232|PYRF_METTH Orotidine 5'-phosphate decarboxylase (Gene Name=pyrF)

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