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8VHM

Structure of DHODH in Complex with Fragment 2

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0004151molecular_functiondihydroorotase activity
A0004152molecular_functiondihydroorotate dehydrogenase activity
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
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
A0016491molecular_functionoxidoreductase activity
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
AGLY114-ARG133

site_idPS00912
Number of Residues21
DetailsDHODEHASE_2 Dihydroorotate dehydrogenase signature 2. IIGvGGVsSgqdAleKIrAGA
ChainResidueDetails
AILE330-ALA350

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues364
DetailsTOPO_DOM: Mitochondrial intermembrane => ECO:0000250
ChainResidueDetails
ATHR32-ARG396

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile
ChainResidueDetails
ASER215

site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:10673429, ECO:0000269|PubMed:16480261
ChainResidueDetails
AALA96
ASER120
AASN181
AASN212
ALYS255
ATHR283
AGLY306
AGLY335
ATYR356

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING:
ChainResidueDetails
ALYS100
AASN145
AASN284

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 109
ChainResidueDetails
AASN145electrostatic stabiliser
APHE149activator, electrostatic stabiliser, enhance reactivity, polar/non-polar interaction
ASER215electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar/non-polar interaction, proton acceptor, proton donor, proton relay
AASN217electrostatic stabiliser
ATHR218activator, electrostatic stabiliser, enhance reactivity, hydrogen bond acceptor
ALYS255electrostatic stabiliser, hydrogen bond donor
AASN284electrostatic stabiliser

219869

PDB entries from 2024-05-15

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