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2ZYL

Crystal structure of 3-ketosteroid-9-alpha-hydroxylase (KshA) from M. tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0006694biological_processsteroid biosynthetic process
A0006707biological_processcholesterol catabolic 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
A0047086molecular_functionketosteroid monooxygenase activity
A0051537molecular_function2 iron, 2 sulfur cluster binding
A0070207biological_processprotein homotrimerization
A0070723biological_processresponse to cholesterol
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES A 451
ChainResidue
ACYS67
AHIS69
AMET70
AGLY72
ACYS86
APHE88
AHIS89
ATRP91

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE2 A 452
ChainResidue
AHIS186
AASP304
AHOH561
AHIS181

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 387
ChainResidue
ATHR177
AASP178
AMET179
AGLU322
AASP323
AHOH435

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00628, ECO:0000269|PubMed:19234303, ECO:0000269|PubMed:25049233
ChainResidueDetails
ACYS67
AHIS69
ACYS86
AHIS89

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:F1CMY8
ChainResidueDetails
AASN175

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:19234303, ECO:0000269|PubMed:25049233
ChainResidueDetails
AHIS181
AHIS186
AASP304

220113

PDB entries from 2024-05-22

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