Structure of PDB 3n34 Chain B

Receptor sequence
>3n34B (length=322) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence]
SMGFKVKLEKRRNAINTCLCIGLDPDEKDIENFMKNEKENNYNNIKKNLK
EKYINNVSIKKDILLKAPDNIIREEKSEEFFYFFNHFCFYIINETNKYAL
TFKMNFAFYIPYGSVGIDVLKNVFDYLYELNIPTILDMKINDIGNTVKNY
RKFIFEYLKSDSCTVNIYMGTNMLKDICYDEEKNKYYSAFVLVKTTNPDS
AIFQKNLSLDNKQAYVIMAQEALNMSSYLNLEQNNEFIGFVVGANSYDEM
NYIRTYFPNCYILSPGIGAQNGDLHKTLTNGYHKSYEKILINIGRAITKN
PYPQKAAQMYYDQINAILKQNM
3D structure
PDB3n34 Crystal structure of Plasmodium falciparum orotidine 5'-monophosphate decarboxylase complexed with 5-fluoro-6-amino-UMP, produced from 5-fluoro-6-azido-UMP
ChainB
Resolution1.55 Å
3D
structure
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Enzymatic activity
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 FNU B D141 I142 T145 D142 I143 T146
BS02 FNU B D23 K102 N104 D136 K138 T194 T195 P264 Q269 G293 R294 D24 K103 N105 D137 K139 T195 T196 P265 Q270 G294 R295
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:0044205 'de novo' UMP biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3n34, PDBe:3n34, PDBj:3n34
PDBsum3n34
PubMed
UniProtQ8IJH3

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