Structure of PDB 1dbt Chain A

Receptor sequence
>1dbtA (length=237) Species: 1423 (Bacillus subtilis) [Search protein sequence]
MKNNLPIIALDFASAEETLAFLAPFQQEPLFVKVGMELFYQEGPSIVKQL
KERNCELFLDLKLHDIPTTVNKAMKRLASLGVDLVNVHAAGGKKMMQAAL
EGLEEGTPAGKKRPSLIAVTQLTSTSEQIMKDELLIEKSLIDTVVHYSKQ
AEESGLDGVVCSVHEAKAIYQAVSPSFLTVTPGIRMSEDAANDQVRVATP
AIAREKGSSAIVVGRSITKAEDPVKAYKAVRLEWEGI
3D structure
PDB1dbt The crystal structure and mechanism of orotidine 5'-monophosphate decarboxylase.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K33 D60 K62 D65 T123 R215
Catalytic site (residue number reindexed from 1) K33 D60 K62 D65 T123 R215
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 U5P A D11 K33 D60 K62 L122 T123 P182 R185 Q194 G214 R215 D11 K33 D60 K62 L122 T123 P182 R185 Q194 G214 R215 MOAD: Ki=0.46mM
BS02 U5P A D65 I66 T69 D65 I66 T69 MOAD: Ki=0.46mM
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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Cellular Component
External links
PDB RCSB:1dbt, PDBe:1dbt, PDBj:1dbt
PDBsum1dbt
PubMed10681442
UniProtP25971|PYRF_BACSU Orotidine 5'-phosphate decarboxylase (Gene Name=pyrF)

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