Structure of PDB 4wzh Chain A

Receptor sequence
>4wzhA (length=304) Species: 5660 (Leishmania braziliensis) [Search protein sequence]
MSLQVGILGNTFANPFMNAAGVMCSTEEELAAMTESTSGSLITKSCTPAL
REGNPAPRYYTLPLGSINSMGLPNKGFDFYLAYSARHHDYSRKPLFISIS
GFSAEENAEMCKRLAPVAAEKGVILELNLSQVAYDFDAMRRYLAAISEAY
PHPFGVKMPPYFDFAHFDAAAEILNQFPKVQFITCINSIGNGLVIDVETE
SVVIKPKQGFGGLGGRYVFPTALANVNAFYRRCPGKLIFGCGGVYTGEDA
FLHVLAGASMVQVGTALHEEGAAIFERLTAELLDVMAKKGYKALDEFRGK
VKAM
3D structure
PDB4wzh Recombinant production, crystallization and crystal structure determination of dihydroorotate dehydrogenase from Leishmania (Viannia) braziliensis.
ChainA
Resolution2.12 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 N68 L72 K165 I194
Catalytic site (residue number reindexed from 1) K44 N68 L72 K157 I186
Enzyme Commision number 1.3.98.1: dihydroorotate oxidase (fumarate).
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 FMN A A19 A20 G21 K44 S45 Y59 N68 M70 N128 K165 I194 N195 G223 C249 G250 G251 G272 T273 A19 A20 G21 K44 S45 Y59 N68 M70 N128 K157 I186 N187 G215 C241 G242 G243 G264 T265
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004152 dihydroorotate dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
GO:1990663 dihydroorotate dehydrogenase (fumarate) activity
Biological Process
GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process
GO:0006221 pyrimidine nucleotide biosynthetic process
GO:0006222 UMP biosynthetic process
GO:0044205 'de novo' UMP biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4wzh, PDBe:4wzh, PDBj:4wzh
PDBsum4wzh
PubMed25945707
UniProtE9AI53

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