Structure of PDB 4zl1 Chain A

Receptor sequence
>4zl1A (length=365) Species: 9606 (Homo sapiens) [Search protein sequence]
TGDERFYAEHLMPTLQGLLDPESAHRLAVRFTSLGLLPRARFQDSDMLEV
RVLGHKFRNPVGIAAGFDKHGEAVDGLYKMGFGFVEIGSVTPKPQEGNPR
PRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAKLTEDGLPLGVN
LGKNKTSVDAAEDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQGKAELR
RLLTKVLQERDGLRRVHRPAVLVKIAPDLTSQDKEDIASVVKELGIDGLI
VTNTTVSRPAGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGRVPII
GVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALLKEQ
GFGGVTDAIGADHRR
3D structure
PDB4zl1 Crystal structure of human dihydroorotate dehydrogenase (DHODH) with 18XYW at 1.86 A resolution
ChainA
Resolution1.86 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G119 N145 F149 S215 N217 T218 K255 N284
Catalytic site (residue number reindexed from 1) G88 N114 F118 S184 N186 T187 K224 N253
Enzyme Commision number 1.3.5.2: dihydroorotate dehydrogenase (quinone).
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004151 dihydroorotase activity
GO:0004152 dihydroorotate dehydrogenase activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
GO:0106430 dihydroorotate dehydrogenase (quinone) activity
Biological Process
GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process
GO:0006221 pyrimidine nucleotide biosynthetic process
GO:0006225 UDP biosynthetic process
GO:0009220 pyrimidine ribonucleotide biosynthetic process
GO:0044205 'de novo' UMP biosynthetic process
Cellular Component
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0005829 cytosol
GO:0016020 membrane

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4zl1, PDBe:4zl1, PDBj:4zl1
PDBsum4zl1
PubMed
UniProtQ02127|PYRD_HUMAN Dihydroorotate dehydrogenase (quinone), mitochondrial (Gene Name=DHODH)

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