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4TRI

X-ray crystal structure of CYP142A2 from Mycobacterium smegmatis, complexed with cholesterol sulfate.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0006707biological_processcholesterol catabolic process
A0008203biological_processcholesterol metabolic process
A0016042biological_processlipid catabolic process
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0006707biological_processcholesterol catabolic process
B0008203biological_processcholesterol metabolic process
B0016042biological_processlipid catabolic process
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue HEM A 501
ChainResidue
AGLU56
ATHR238
AVAL280
AARG285
AALA335
APHE336
AGLY337
APHE338
AHIS341
ACYS343
ALEU344
AILE79
AGLY345
ALEU348
AC3S502
AHOH667
AHIS86
AARG90
APHE97
AILE141
AGLY233
AGLY234
ATHR237

site_idAC2
Number of Residues5
Detailsbinding site for residue C3S A 502
ChainResidue
ATYR77
AMET179
ALEU229
AHEM501
AHOH812

site_idAC3
Number of Residues8
Detailsbinding site for residue GOL A 503
ChainResidue
AGLU122
ALEU145
AGLY146
AARG196
AASP203
AHIS402
AHOH601
AHOH614

site_idAC4
Number of Residues7
Detailsbinding site for residue C3S B 501
ChainResidue
BTYR77
BMET179
BLEU229
BPHE382
BHEM502
BHOH746
BHOH924

site_idAC5
Number of Residues23
Detailsbinding site for residue HEM B 502
ChainResidue
BGLU56
BILE79
BHIS86
BARG90
BPHE97
BILE230
BGLY233
BTHR237
BTHR238
BTHR241
BPRO279
BVAL280
BARG285
BALA335
BPHE336
BGLY337
BPHE338
BHIS341
BCYS343
BLEU344
BGLY345
BC3S501
BHOH669

site_idAC6
Number of Residues6
Detailsbinding site for residue GOL B 503
ChainResidue
BLEU145
BGLY146
BGLU151
BVAL192
BARG196
BASP203

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 Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:23489718, ECO:0000269|PubMed:25210044, ECO:0007744|PDB:2YOO, ECO:0007744|PDB:3ZBY, ECO:0007744|PDB:4TRI, ECO:0007744|PDB:4UAX
ChainResidueDetails
ACYS343
BCYS343

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PDB entries from 2024-07-31

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