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7Z6C

Crystal structure of human Dihydroorotate Dehydrogenase in complex with the inhibitor 2-Hydroxy-N-(2-ispropyl-5-methyl-4-phenoxyphenyl)pyrazolo[1,5-a]pyridine-3-carboxamide.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004151molecular_functiondihydroorotase activity
A0004152molecular_functiondihydroorotate dehydrogenase activity
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005829cellular_componentcytosol
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0006225biological_processUDP biosynthetic process
A0009220biological_processpyrimidine ribonucleotide biosynthetic process
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0044205biological_process'de novo' UMP biosynthetic process
A0106430molecular_functiondihydroorotate dehydrogenase (quinone) activity
Functional Information from PROSITE/UniProt
site_idPS00911
Number of Residues20
DetailsDHODEHASE_1 Dihydroorotate dehydrogenase signature 1. GfveiGSVTpkpQeGNprPR
ChainResidueDetails
AGLY113-ARG132

site_idPS00912
Number of Residues21
DetailsDHODEHASE_2 Dihydroorotate dehydrogenase signature 2. IIGvGGVsSgqdAleKIrAGA
ChainResidueDetails
AILE329-ALA349

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues364
DetailsTOPO_DOM: Mitochondrial intermembrane => ECO:0000250
ChainResidueDetails
ATHR31-ARG395

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile
ChainResidueDetails
ASER214

site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:10673429, ECO:0000269|PubMed:16480261
ChainResidueDetails
AALA95
ASER119
AASN180
AASN211
ALYS254
ATHR282
AGLY305
AGLY334
ATYR355

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING:
ChainResidueDetails
ALYS99
AASN144
AASN283

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 109
ChainResidueDetails
AASN144electrostatic stabiliser
APHE148activator, electrostatic stabiliser, enhance reactivity, polar/non-polar interaction
ASER214electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar/non-polar interaction, proton acceptor, proton donor, proton relay
AASN216electrostatic stabiliser
ATHR217activator, electrostatic stabiliser, enhance reactivity, hydrogen bond acceptor
ALYS254electrostatic stabiliser, hydrogen bond donor
AASN283electrostatic stabiliser

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PDB entries from 2024-06-12

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