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6SYP

Human DHODH bound to inhibitor IPP/CNRS-A017

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0004151molecular_functiondihydroorotase activity
AAA0004152molecular_functiondihydroorotate dehydrogenase activity
AAA0005515molecular_functionprotein binding
AAA0005654cellular_componentnucleoplasm
AAA0005737cellular_componentcytoplasm
AAA0005739cellular_componentmitochondrion
AAA0005743cellular_componentmitochondrial inner membrane
AAA0005829cellular_componentcytosol
AAA0005886cellular_componentplasma membrane
AAA0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
AAA0006221biological_processpyrimidine nucleotide biosynthetic process
AAA0006225biological_processUDP biosynthetic process
AAA0009220biological_processpyrimidine ribonucleotide biosynthetic process
AAA0016020cellular_componentmembrane
AAA0016491molecular_functionoxidoreductase activity
AAA0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
AAA0044205biological_process'de novo' UMP biosynthetic process
AAA0106430molecular_functiondihydroorotate dehydrogenase (quinone) activity
Functional Information from PROSITE/UniProt
site_idPS00911
Number of Residues20
DetailsDHODEHASE_1 Dihydroorotate dehydrogenase signature 1. GfveiGSVTpkpQeGNprPR
ChainResidueDetails
AAAGLY114-ARG133

site_idPS00912
Number of Residues21
DetailsDHODEHASE_2 Dihydroorotate dehydrogenase signature 2. IIGvGGVsSgqdAleKIrAGA
ChainResidueDetails
AAAILE330-ALA350

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsTOPO_DOM: Mitochondrial matrix => ECO:0000250
ChainResidueDetails
AAAMET2-ALA11

site_idSWS_FT_FI2
Number of Residues19
DetailsTRANSMEM: Helical => ECO:0000250
ChainResidueDetails
AAAGLN12-ALA31

site_idSWS_FT_FI3
Number of Residues364
DetailsTOPO_DOM: Mitochondrial intermembrane => ECO:0000250
ChainResidueDetails
AAATHR32-ARG396

site_idSWS_FT_FI4
Number of Residues1
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AAASER215

site_idSWS_FT_FI5
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:10673429, ECO:0000269|PubMed:16480261
ChainResidueDetails
AAAALA96
AAASER120
AAAASN181
AAAASN212
AAALYS255
AAATHR283
AAAGLY306
AAAGLY335
AAATYR356

site_idSWS_FT_FI6
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AAALYS100
AAAASN145
AAAASN284

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 109
ChainResidueDetails
AAAASN145electrostatic stabiliser
AAAPHE149activator, electrostatic stabiliser, enhance reactivity, polar/non-polar interaction
AAASER215electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar/non-polar interaction, proton acceptor, proton donor, proton relay
AAAASN217electrostatic stabiliser
AAATHR218activator, electrostatic stabiliser, enhance reactivity, hydrogen bond acceptor
AAALYS255electrostatic stabiliser, hydrogen bond donor
AAAASN284electrostatic stabiliser

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PDB entries from 2024-04-24

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