Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2JBT

Structure of the monooxygenase component of p-hydroxyphenylacetate hydroxylase from Acinetobacter baumannii

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003995molecular_functionacyl-CoA dehydrogenase activity
A0004497molecular_functionmonooxygenase activity
A0005737cellular_componentcytoplasm
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0016712molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
A0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
A0050660molecular_functionflavin adenine dinucleotide binding
A0052881molecular_function4-hydroxyphenylacetate 3-monooxygenase activity
B0000166molecular_functionnucleotide binding
B0003995molecular_functionacyl-CoA dehydrogenase activity
B0004497molecular_functionmonooxygenase activity
B0005737cellular_componentcytoplasm
B0016491molecular_functionoxidoreductase activity
B0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
B0016712molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
B0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
B0050660molecular_functionflavin adenine dinucleotide binding
B0052881molecular_function4-hydroxyphenylacetate 3-monooxygenase activity
C0000166molecular_functionnucleotide binding
C0003995molecular_functionacyl-CoA dehydrogenase activity
C0004497molecular_functionmonooxygenase activity
C0005737cellular_componentcytoplasm
C0016491molecular_functionoxidoreductase activity
C0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
C0016712molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
C0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
C0050660molecular_functionflavin adenine dinucleotide binding
C0052881molecular_function4-hydroxyphenylacetate 3-monooxygenase activity
D0000166molecular_functionnucleotide binding
D0003995molecular_functionacyl-CoA dehydrogenase activity
D0004497molecular_functionmonooxygenase activity
D0005737cellular_componentcytoplasm
D0016491molecular_functionoxidoreductase activity
D0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
D0016712molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
D0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
D0050660molecular_functionflavin adenine dinucleotide binding
D0052881molecular_function4-hydroxyphenylacetate 3-monooxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE FMN A1423
ChainResidue
ATRP112
AHIS396
AALA397
A4HP1424
DARG292
DTYR296
DGLY373
DALA374
DTHR375
ALEU116
ASER146
ASER147
AILE148
ATRP169
ASER170
ASER171
ASER220

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 4HP A1424
ChainResidue
ALEU116
AHIS120
ASER146
AILE148
AARG263
APHE266
AALA267
ATYR398
AFMN1423
DTYR296

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE FMN B1423
ChainResidue
BTRP112
BLEU116
BSER146
BSER147
BILE148
BTRP169
BSER171
BSER220
BHIS396
BALA397
B4HP1424
CARG292
CTYR296
CGLY373
CALA374
CTHR375

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 4HP B1424
ChainResidue
BLEU116
BHIS120
BSER146
BILE148
BARG263
BPHE266
BALA267
BTYR398
BFMN1423
CTYR296

site_idAC5
Number of Residues16
DetailsBINDING SITE FOR RESIDUE FMN C1423
ChainResidue
BARG292
BTYR296
BGLY373
BALA374
BTHR375
CTRP112
CSER146
CSER147
CILE148
CTRP169
CSER170
CSER171
CSER220
CHIS396
CALA397
C4HP1424

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 4HP C1424
ChainResidue
BTYR296
CLEU116
CHIS120
CSER146
CILE148
CARG263
CPHE266
CALA267
CTYR398
CFMN1423

site_idAC7
Number of Residues17
DetailsBINDING SITE FOR RESIDUE FMN D1423
ChainResidue
AARG292
ATYR296
AGLY373
AALA374
ATHR375
DTRP112
DLEU116
DSER146
DSER147
DILE148
DTRP169
DSER170
DSER171
DSER220
DHIS396
DALA397
D4HP1424

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 4HP D1424
ChainResidue
DILE148
DARG263
DPHE266
DALA267
DTYR398
DFMN1423
DLEU116
DHIS120
DSER146

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues32
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17227849","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues24
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
APHE266

site_idCSA10
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
BTHR260

site_idCSA11
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
CTHR260

site_idCSA12
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
DTHR260

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
BPHE266

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
CPHE266

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
DPHE266

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
AALA397

site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
BALA397

site_idCSA7
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
CALA397

site_idCSA8
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
DALA397

site_idCSA9
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
ATHR260

238895

PDB entries from 2025-07-16

PDB statisticsPDBj update infoContact PDBjnumon