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1DOC

THE MOBIL FLAVIN OF 4-OH BENZOATE HYDROXYLASE: MOTION OF A PROSTHETIC GROUP REGULATES CATALYSIS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0009056biological_processcatabolic process
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 PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BR A 397
ChainResidue
AARG44
AALA45
AGLN102
ATHR103
AARG214

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BR A 398
ChainResidue
APRO293
ALYS297
AGLY298
AFAD395

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BR A 519
ChainResidue
ALYS297
AARG335
ALEU388
AHOH520

site_idAC4
Number of Residues33
DetailsBINDING SITE FOR RESIDUE FAD A 395
ChainResidue
AILE8
AGLY9
AGLY11
APRO12
ASER13
ALEU31
AGLU32
AARG33
AARG42
AARG44
AALA45
AGLY46
AVAL47
AGLN102
ACYS158
AASP159
AGLY160
AGLY163
AGLY285
AASP286
AALA296
ALYS297
AGLY298
ALEU299
AASN300
APHB396
ABR398
AHOH407
AHOH408
AHOH409
AHOH410
AHOH418
AHOH475

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PHB A 396
ChainResidue
AARG44
AGLY46
ATYR201
ASER212
AARG214
ATYR222
APRO293
ATHR294
AALA296
AFAD395

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:10600126, ECO:0000269|PubMed:11805318, ECO:0000269|PubMed:15924424, ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276, ECO:0000269|PubMed:8555229
ChainResidueDetails
ASER13
AGLU32
AARG42
AGLN102
ATYR201
ASER212
ATYR222
APRO293
ALEU299

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10600126, ECO:0000269|PubMed:15924424, ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276, ECO:0000269|PubMed:8555229
ChainResidueDetails
AASP286

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0000269|PubMed:8312276
ChainResidueDetails
ATYR201
ATYR385

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dod
ChainResidueDetails
ATYR201
ATYR385

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 2024-09-18

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