Structure of PDB 1jjk Chain A

Receptor sequence
>1jjkA (length=231) Species: 562 (Escherichia coli) [Search protein sequence]
VTNSPVVVALDYHNRDDALAFVDKIDPRDCRLKVGKEMFTLFGPQFVREL
QQRGFDIFLDLKFHDIPNTAAHAVAAAADLGVWMVNVHASGGARMMTAAR
EALVPFGKDAPLLIAVTVLTSMEASDLVDLGMTLSPADYAERLAALTQKC
GLDGVVCSAQEAVRFKQVFGQEFKLVTPGIRPQGSEAGDQRRIMTPEQAL
SAGVDYMVIGRPVTQSVDPAQTLKAINASLQ
3D structure
PDB1jjk Selenomethionine substitution of orotidine-5'-monophosphate decarboxylase causes a change in crystal contacts and space group.
ChainA
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K44 D71 K73 D76 T131 R222
Catalytic site (residue number reindexed from 1) K33 D60 K62 D65 T120 R211
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 A20 D22 K44 K73 L130 T131 P189 R192 Q201 G221 R222 A9 D11 K33 K62 L119 T120 P178 R181 Q190 G210 R211 PDBbind-CN: -logKd/Ki=11.06,Ki=8.8pM
BS02 BMP A D76 I77 T80 D65 I66 T69 PDBbind-CN: -logKd/Ki=11.06,Ki=8.8pM
Gene Ontology
Molecular Function
GO:0004590 orotidine-5'-phosphate decarboxylase activity
GO:0005515 protein binding
GO:0016831 carboxy-lyase activity
Biological Process
GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process
GO:0006221 pyrimidine nucleotide biosynthetic process
GO:0015949 nucleobase-containing small molecule interconversion
GO:0044205 'de novo' UMP biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:1jjk, PDBe:1jjk, PDBj:1jjk
PDBsum1jjk
PubMed11526316
UniProtP08244|PYRF_ECOLI Orotidine 5'-phosphate decarboxylase (Gene Name=pyrF)

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