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1U13

Crystal structure analysis of the C37L/C151T/C442A-triple mutant of CYP51 from Mycobacterium tuberculosis

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
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM A 460
ChainResidue
AGLN72
AARG326
APRO386
APHE387
AGLY388
AHIS392
ACYS394
AVAL395
AGLY396
AALA400
AHOH500
ATYR76
ALYS97
AHIS101
ALEU105
AALA256
AGLY257
ATHR260
APRO320

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 Residues5
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
ATYR76
ALYS97
AARG326
AHIS392

site_idSWS_FT_FI2
Number of Residues1
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

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

226707

PDB entries from 2024-10-30

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