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4QDD

Crystal structure of 3-ketosteroid-9-alpha-hydroxylase 5 (KshA5) from R. rhodochrous in complex with 1,4-30Q-CoA

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0006629biological_processlipid metabolic process
A0006707biological_processcholesterol catabolic process
A0008202biological_processsteroid metabolic process
A0008203biological_processcholesterol metabolic process
A0016042biological_processlipid catabolic process
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0036200molecular_function3-ketosteroid 9-alpha-monooxygenase activity
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES A 401
ChainResidue
ACYS73
AHIS75
AMET76
AGLY78
ACYS92
APHE94
AHIS95
ATRP97

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE2 A 402
ChainResidue
AHIS192
AASP311
AHOH501
AHIS187

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 30Q A 403
ChainResidue
AASN181
AVAL182
AHIS192
AGLN210
ASER235
AASP247
AGLN299
APHE300

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00628, ECO:0000269|PubMed:25049233
ChainResidueDetails
ACYS73
AHIS75
ACYS92
AHIS95

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:25049233
ChainResidueDetails
AASN181
AHIS187
AHIS192
AASP311

218853

PDB entries from 2024-04-24

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