Structure of PDB 3rlu Chain A

Receptor sequence
>3rluA (length=220) Species: 187420 (Methanothermobacter thermautotrophicus str. Delta H) [Search protein sequence]
DVMDVMNRLILAMDLMNRDDALRVTGEVREYIDTVKIGYPLVLSEGMDII
AEFRKRFGCRIIADFKVADIPETNEAICRATFKAGADAIIVHGFPGADSV
RACLNVAEEMGREVFLLTEMSHPGAEMFIQGAADEIARMGVDLGVKNYVG
PSTRPERLSRLREIIGQDSFLISPGVGAQGGDPGETLRFADAIIVGRSIY
LADNPAAAAAGIIESIKDLL
3D structure
PDB3rlu Conformational changes in orotidine 5'-monophosphate decarboxylase: a structure-based explanation for how the 5'-phosphate group activates the enzyme.
ChainA
Resolution1.49 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) K36 D64 K66 D69
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 BMP A D20 K72 M126 S127 P180 Q185 G202 R203 D14 K66 M120 S121 P174 Q179 G196 R197
BS02 BMP A D75 I76 T79 D69 I70 T73
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:3rlu, PDBe:3rlu, PDBj:3rlu
PDBsum3rlu
PubMed23030629
UniProtO26232|PYRF_METTH Orotidine 5'-phosphate decarboxylase (Gene Name=pyrF)

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