1U13
Crystal structure analysis of the C37L/C151T/C442A-triple mutant of CYP51 from Mycobacterium tuberculosis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006694 | biological_process | steroid biosynthetic process |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0008398 | molecular_function | sterol 14-demethylase activity |
| A | 0016125 | biological_process | sterol metabolic process |
| A | 0016126 | biological_process | sterol biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEM A 460 |
| Chain | Residue |
| A | GLN72 |
| A | ARG326 |
| A | PRO386 |
| A | PHE387 |
| A | GLY388 |
| A | HIS392 |
| A | CYS394 |
| A | VAL395 |
| A | GLY396 |
| A | ALA400 |
| A | HOH500 |
| A | TYR76 |
| A | LYS97 |
| A | HIS101 |
| A | LEU105 |
| A | ALA256 |
| A | GLY257 |
| A | THR260 |
| A | PRO320 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGaGRHRCVG |
| Chain | Residue | Details |
| A | PHE387-GLY396 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11248033","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15530358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17846131","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18367444","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19190730","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2004","submissionDatabase":"PDB data bank","title":"Crystal structure analysis of the C37L/C151T/C442A-triple mutant of CYP51 from Mycobacterium tuberculosis.","authors":["Podust L.M.","Yermalitskaya L.V.","Kim Y.","Waterman M.R."]}},{"source":"PDB","id":"1E9X","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1X8V","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"11248033","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15530358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17846131","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18367444","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19190730","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2004","submissionDatabase":"PDB data bank","title":"Crystal structure analysis of the C37L/C151T/C442A-triple mutant of CYP51 from Mycobacterium tuberculosis.","authors":["Podust L.M.","Yermalitskaya L.V.","Kim Y.","Waterman M.R."]}},{"source":"PDB","id":"1E9X","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1X8V","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| A | HIS259 | |
| A | THR260 |
