Structure of PDB 2rfq Chain D

Receptor sequence

>2rfqD (length=379) Species: 101510 (Rhodococcus jostii RHA1)

HDSHEVMQRLDALLPTLRERAQETEDLRRIPDDSMKALQETGFFRLLQPE
QWGGYQADPVLFYSAVRKIASACGSTGWVSSIIGVHNWHLALFSQQAQED
VWGNDTDVRISSSYAPMGAGQVVDGGYTVNGAWAWSSGCDHASWAVLGGP
VIKDGRPVDFVSFLIPREDYRIDDVWNVVGLRGTGSNTVVVEDVFVPTHR
VLSFKAMSNLTAPGLERNTAPVYKMPWGTIHPTTISAPIVGMAYGAYDAH
VEHQGKRVRDDPFAKVRIAEASSDIDAAWRQLSGNVADEYALLVAGEEVP
FELRLRARRDQVRATGRAISSIDKLFESSGATALANGTPLQRFWRDAHAG
RVHAANDPERAYVMYGTGEFGLPITDTMV

3D structure

• PDB: 2rfq Crystal structure of 3-HSA hydroxylase, oxygenase from Rhodococcus sp. RHA1.
• Chain: D
• Resolution: 1.65 Å

Enzymatic activity

• Enzyme Commision number: 1.14.14.12: 3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione monooxygenase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	1PS	D	D162 S206 K208	D159 S203 K205
BS02	1PS	D	R170 R174	R167 R171
BS03	1PS	D	G56 Y58	G53 Y55

Gene Ontology

Molecular Function

• GO:0003995 acyl-CoA dehydrogenase activity
• GO:0004497 monooxygenase activity
• GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
• GO:0036383 3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione monooxygenase activity
• GO:0050660 flavin adenine dinucleotide binding

Biological Process

• GO:0006694 steroid biosynthetic process
• GO:0008202 steroid metabolic process
• GO:0016042 lipid catabolic process
• GO:0033539 fatty acid beta-oxidation using acyl-CoA dehydrogenase

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:2rfq, PDBe:2rfq, PDBj:2rfq
• PDBsum: 2rfq
• UniProt: Q0S811|HSAA_RHOJR Flavin-dependent monooxygenase, oxygenase subunit HsaA (Gene Name=hsaA)