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3RP8

Crystal Structure of Klebsiella pneumoniae R204Q HpxO complexed with FAD

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0004846molecular_functionurate oxidase activity
A0006144biological_processpurine nucleobase metabolic process
A0016709molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
A0019628biological_processurate catabolic process
A0071949molecular_functionFAD binding
A0102099molecular_functionFAD-dependent urate hydroxylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues32
DetailsBINDING SITE FOR RESIDUE FAD A 385
ChainResidue
AILE6
ASER43
AARG103
ALYS123
AARG124
AVAL125
AALA153
AASP154
AGLY155
AGLY284
AASP285
AGLY7
APRO292
AGLY295
AGLY297
AGLY298
ACYS299
ACL386
AHOH393
AHOH438
AHOH439
AHOH440
AGLY9
AHOH453
AHOH478
AHOH483
AILE10
AGLY11
AGLU30
AALA31
AVAL32
AILE42

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 386
ChainResidue
APRO292
AGLN296
AGLY297
AFAD385
AHOH418

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:23259842, ECO:0007744|PDB:3RP6, ECO:0007744|PDB:3RP7, ECO:0007744|PDB:3RP8
ChainResidueDetails
AGLY11
AGLU30
ASER43
AVAL125
AASP285
AGLY295

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:23259842, ECO:0007744|PDB:3RP7
ChainResidueDetails
AASN178
AGLN204
ATYR216

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Involved in substrate activation for the transfer of oxygen from the flavin hydroperoxide => ECO:0000305|PubMed:23259842
ChainResidueDetails
AGLN204

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PDB entries from 2024-07-10

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