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2RFQ

Crystal structure of 3-HSA hydroxylase from Rhodococcus sp. RHA1

Functional Information from GO Data
ChainGOidnamespacecontents
A0003995molecular_functionacyl-CoA dehydrogenase activity
A0004497molecular_functionmonooxygenase activity
A0005737cellular_componentcytoplasm
A0006629biological_processlipid metabolic process
A0006694biological_processsteroid biosynthetic process
A0008202biological_processsteroid metabolic process
A0016042biological_processlipid catabolic process
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
A0036383molecular_function3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione monooxygenase activity
A0050660molecular_functionflavin adenine dinucleotide binding
B0003995molecular_functionacyl-CoA dehydrogenase activity
B0004497molecular_functionmonooxygenase activity
B0005737cellular_componentcytoplasm
B0006629biological_processlipid metabolic process
B0006694biological_processsteroid biosynthetic process
B0008202biological_processsteroid metabolic process
B0016042biological_processlipid catabolic process
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
B0036383molecular_function3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione monooxygenase activity
B0050660molecular_functionflavin adenine dinucleotide binding
C0003995molecular_functionacyl-CoA dehydrogenase activity
C0004497molecular_functionmonooxygenase activity
C0005737cellular_componentcytoplasm
C0006629biological_processlipid metabolic process
C0006694biological_processsteroid biosynthetic process
C0008202biological_processsteroid metabolic process
C0016042biological_processlipid catabolic process
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
C0036383molecular_function3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione monooxygenase activity
C0050660molecular_functionflavin adenine dinucleotide binding
D0003995molecular_functionacyl-CoA dehydrogenase activity
D0004497molecular_functionmonooxygenase activity
D0005737cellular_componentcytoplasm
D0006629biological_processlipid metabolic process
D0006694biological_processsteroid biosynthetic process
D0008202biological_processsteroid metabolic process
D0016042biological_processlipid catabolic process
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
D0036383molecular_function3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione monooxygenase activity
D0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 1PS C 392
ChainResidue
CVAL161
CASP162
CPHE163
CSER206
CLYS208
CHOH554
CHOH704
CHOH768

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 1PS D 392
ChainResidue
DASP162
DPHE163
DSER206
DLYS208
DHOH460
DHOH768
DHOH795
DVAL161

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 1PS D 393
ChainResidue
CSER97
CTYR130
CTHR201
CHIS202
CVAL204
CHOH560
CHOH602

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 1PS A 392
ChainResidue
AHIS256
ATHR344
APRO351
ALEU352
AHOH446

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE 1PS C 393
ChainResidue
CASP127
CPHE198

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 1PS A 393
ChainResidue
AARG170
ATYR173
AARG174
AILE175
AHOH525

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 1PS C 394
ChainResidue
CARG170
CTYR173
CARG174
CILE175
CHOH420
CHOH731

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 1PS B 392
ChainResidue
BHIS256
BTHR344
BPRO351
BLEU352
BHOH410

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 1PS C 395
ChainResidue
CHIS256
CTHR344
CPRO351
CLEU352
CHOH462

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 1PS D 394
ChainResidue
DARG170
DTYR173
DARG174
DILE175
DHOH458
DHOH569

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE 1PS B 394
ChainResidue
BGLU8
BGLY56
BTYR58

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE 1PS D 395
ChainResidue
DGLY56
DTYR58

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues32
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
AGLY231

site_idCSA10
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
BTHR236

site_idCSA11
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
CTHR236

site_idCSA12
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
DTHR236

site_idCSA13
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
AALA366

site_idCSA14
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
BALA366

site_idCSA15
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
CALA366

site_idCSA16
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
DALA366

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
BGLY231

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
CGLY231

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
DGLY231

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
AILE242

site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
BILE242

site_idCSA7
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
CILE242

site_idCSA8
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
DILE242

site_idCSA9
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
ATHR236

243911

PDB entries from 2025-10-29

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