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8Y2S

P-hydroxybenzoate hydroxylase complexed with 4-hydroxy-3-methylbenzoic acid

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0016491molecular_functionoxidoreductase activity
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
A0018659molecular_function4-hydroxybenzoate 3-monooxygenase activity
A0043639biological_processbenzoate catabolic process
A0043640biological_processbenzoate catabolic process via hydroxylation
A0050660molecular_functionflavin adenine dinucleotide binding
A0071949molecular_functionFAD binding
A0106356molecular_function4-hydroxybenzoate 3-monooxygenase (NADPH) activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10600126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11805318","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15924424","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7939628","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8312276","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8555229","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10600126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15924424","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7939628","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8312276","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8555229","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"source":"PubMed","id":"8312276","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 131
ChainResidueDetails
AHIS72hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
ATYR201hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
APRO293electrostatic stabiliser, hydrogen bond acceptor
ALYS297attractive charge-charge interaction, electrostatic stabiliser, steric role
ATYR385hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay

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PDB entries from 2025-10-22

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