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2YOO

Cholest-4-en-3-one bound structure of CYP142 from Mycobacterium smegmatis

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
A0008395molecular_functionsteroid hydroxylase activity
A0016042biological_processlipid catabolic process
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0020037molecular_functionheme binding
A0036199molecular_functioncholest-4-en-3-one 26-monooxygenase activity
A0046872molecular_functionmetal ion binding
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0006629biological_processlipid metabolic process
B0006707biological_processcholesterol catabolic process
B0008202biological_processsteroid metabolic process
B0008203biological_processcholesterol metabolic process
B0008395molecular_functionsteroid hydroxylase activity
B0016042biological_processlipid catabolic process
B0016491molecular_functionoxidoreductase activity
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0020037molecular_functionheme binding
B0036199molecular_functioncholest-4-en-3-one 26-monooxygenase activity
B0046872molecular_functionmetal ion binding
C0004497molecular_functionmonooxygenase activity
C0005506molecular_functioniron ion binding
C0006629biological_processlipid metabolic process
C0006707biological_processcholesterol catabolic process
C0008202biological_processsteroid metabolic process
C0008203biological_processcholesterol metabolic process
C0008395molecular_functionsteroid hydroxylase activity
C0016042biological_processlipid catabolic process
C0016491molecular_functionoxidoreductase activity
C0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C0020037molecular_functionheme binding
C0036199molecular_functioncholest-4-en-3-one 26-monooxygenase activity
C0046872molecular_functionmetal ion binding
D0004497molecular_functionmonooxygenase activity
D0005506molecular_functioniron ion binding
D0006629biological_processlipid metabolic process
D0006707biological_processcholesterol catabolic process
D0008202biological_processsteroid metabolic process
D0008203biological_processcholesterol metabolic process
D0008395molecular_functionsteroid hydroxylase activity
D0016042biological_processlipid catabolic process
D0016491molecular_functionoxidoreductase activity
D0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
D0020037molecular_functionheme binding
D0036199molecular_functioncholest-4-en-3-one 26-monooxygenase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM A 1402
ChainResidue
AGLU56
ATHR238
ATHR241
ALEU274
APRO279
AVAL280
AARG285
AALA335
APHE336
AGLY337
APHE338
AILE79
AHIS341
ACYS343
ALEU344
AGLY345
AK2B1404
AHOH2339
AHIS86
AARG90
AILE141
AILE230
AGLY233
AGLY234
ATHR237

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K2B A 1404
ChainResidue
AGLN72
ATYR77
AMET179
APHE182
ALEU229
AHEM1402

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM B 1402
ChainResidue
BGLU56
BILE79
BHIS86
BARG90
BPHE97
BGLY233
BGLY234
BTHR237
BTHR238
BLEU274
BVAL280
BARG285
BALA335
BPHE336
BGLY337
BPHE338
BHIS341
BCYS343
BGLY345
BALA349
BK2B1404
BHOH2371

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K2B B 1404
ChainResidue
BTYR77
BMET179
BPHE182
BLEU229
BHEM1402

site_idAC5
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM C 1402
ChainResidue
CGLU56
CILE79
CHIS86
CARG90
CILE141
CILE230
CGLY233
CGLY234
CTHR237
CTHR238
CTHR241
CLEU274
CPRO279
CVAL280
CARG285
CALA335
CPHE336
CGLY337
CPHE338
CHIS341
CCYS343
CLEU344
CGLY345
CK2B1404
CHOH2395

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K2B C 1404
ChainResidue
CTYR77
CLEU178
CPHE182
CHEM1402

site_idAC7
Number of Residues28
DetailsBINDING SITE FOR RESIDUE HEM D 1402
ChainResidue
DLEU274
DPRO279
DVAL280
DMET283
DARG285
DALA335
DPHE336
DGLY337
DPHE338
DHIS341
DCYS343
DLEU344
DGLY345
DLEU348
DK2B1404
DHOH2347
DGLU56
DILE79
DHIS86
DARG90
DPHE97
DILE141
DILE230
DGLY233
DGLY234
DTHR237
DTHR238
DTHR241

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K2B D 1404
ChainResidue
DTYR77
DLEU178
DMET179
DPHE182
DLEU229
DHEM1402

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 1405
ChainResidue
BHOH2119
BHOH2151
BHOH2456
BHOH2457
BHOH2458
BHOH2459

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGfGTHFCLG
ChainResidueDetails
APHE336-GLY345

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"23489718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25210044","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2YOO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZBY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TRI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UAX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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