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2BZ9

Ligand-free structure of sterol 14alpha-demethylase from Mycobacterium tuberculosis in P2(1) space group

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008398molecular_functionsterol 14-demethylase activity
A0016125biological_processsterol metabolic process
A0016126biological_processsterol biosynthetic process
A0016491molecular_functionoxidoreductase activity
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
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008398molecular_functionsterol 14-demethylase activity
B0016125biological_processsterol metabolic process
B0016126biological_processsterol biosynthetic process
B0016491molecular_functionoxidoreductase activity
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 Residues17
DetailsBINDING SITE FOR RESIDUE HEM A1449
ChainResidue
AGLN72
APHE387
AGLY388
AHIS392
ACYS394
AVAL395
APHE399
AALA400
AHOH2054
ALEU105
AALA256
AGLY257
ATHR260
ASER261
APRO320
AARG326
APRO386

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEM B1449
ChainResidue
BGLN72
BLEU105
BALA256
BGLY257
BTHR260
BSER261
BTHR264
BPRO320
BLEU324
BARG326
BPRO386
BPHE387
BGLY388
BHIS392
BCYS394
BVAL395
BGLY396
BHOH2016
BHOH2068
BHOH2095
BHOH2114

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGaGRHRCVG
ChainResidueDetails
APHE387-GLY396

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:11248033, ECO:0000269|PubMed:15530358, ECO:0000269|PubMed:17846131, ECO:0000269|PubMed:18367444, ECO:0000269|PubMed:19190730, ECO:0000269|Ref.9, ECO:0007744|PDB:1E9X, ECO:0007744|PDB:1X8V
ChainResidueDetails
AGLN72
BHIS392
ATYR76
ALYS97
AARG326
AHIS392
BGLN72
BTYR76
BLYS97
BARG326

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:11248033, ECO:0000269|PubMed:15530358, ECO:0000269|PubMed:17846131, ECO:0000269|PubMed:18367444, ECO:0000269|PubMed:19190730, ECO:0000269|Ref.9, ECO:0007744|PDB:1E9X, ECO:0007744|PDB:1X8V
ChainResidueDetails
ACYS394
BCYS394

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
AHIS259
ATHR260

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
BHIS259
BTHR260

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PDB entries from 2024-10-09

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