1X74
Alpha-methylacyl-CoA racemase from Mycobacterium tuberculosis- mutational and structural characterization of the fold and active site
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006637 | biological_process | acyl-CoA metabolic process |
| A | 0008111 | molecular_function | alpha-methylacyl-CoA racemase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006637 | biological_process | acyl-CoA metabolic process |
| B | 0008111 | molecular_function | alpha-methylacyl-CoA racemase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0006637 | biological_process | acyl-CoA metabolic process |
| C | 0008111 | molecular_function | alpha-methylacyl-CoA racemase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0042803 | molecular_function | protein homodimerization activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0006637 | biological_process | acyl-CoA metabolic process |
| D | 0008111 | molecular_function | alpha-methylacyl-CoA racemase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 D 1600 |
| Chain | Residue |
| A | HIS282 |
| D | HIS282 |
| D | HOH2345 |
| D | HOH2483 |
| D | HOH2542 |
| D | HOH2543 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL C 2301 |
| Chain | Residue |
| C | ASN103 |
| C | ASP104 |
| C | LEU106 |
| C | GLY181 |
| C | HOH2438 |
| C | HOH2542 |
| C | PRO96 |
| C | CYS99 |
| C | ALA100 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL B 2302 |
| Chain | Residue |
| A | PRO261 |
| A | ASN263 |
| A | ASP264 |
| A | HOH2340 |
| A | HOH2517 |
| B | MET216 |
| B | TYR223 |
| B | ILE240 |
| B | GLN262 |
| B | ASN263 |
| B | HOH2374 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 2303 |
| Chain | Residue |
| A | MET202 |
| A | MET207 |
| A | HOH2506 |
| B | ASP48 |
| B | MET50 |
| B | ALA266 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL B 2304 |
| Chain | Residue |
| B | PRO96 |
| B | CYS99 |
| B | ALA100 |
| B | ASN103 |
| B | ASP104 |
| B | LEU106 |
| B | TYR108 |
| B | GLY181 |
| B | GLN182 |
| B | HOH2433 |
| B | HOH2561 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL D 2305 |
| Chain | Residue |
| C | PRO261 |
| C | ASN263 |
| C | HOH2360 |
| D | MET216 |
| D | ILE240 |
| D | PRO242 |
| D | GLN262 |
| D | ASN263 |
| D | HOH2387 |
| D | HOH2418 |
| D | HOH2525 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GOL D 2306 |
| Chain | Residue |
| C | MET216 |
| C | TYR223 |
| C | ILE240 |
| C | PRO242 |
| C | GLN262 |
| C | ASN263 |
| D | PRO261 |
| D | ASN263 |
| D | HOH2381 |
| D | HOH2384 |
| D | HOH2419 |
| D | HOH2677 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 2307 |
| Chain | Residue |
| C | HIS126 |
| C | ASP127 |
| C | ASP156 |
| C | HOH2390 |
| C | HOH2525 |
| C | HOH2539 |
| C | HOH2662 |
| D | LEU217 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GOL B 2308 |
| Chain | Residue |
| A | MET216 |
| A | ILE240 |
| A | PRO242 |
| A | GLN262 |
| A | ASN263 |
| A | HOH2433 |
| B | PRO261 |
| B | ASN263 |
| B | HOH2340 |
| B | HOH2393 |
| B | HOH2504 |
| B | HOH2640 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 2309 |
| Chain | Residue |
| C | ILE240 |
| D | GLY17 |
| D | HIS126 |
| D | ASP127 |
| D | ASN152 |
| D | ASP156 |
| D | HOH2407 |
| D | HOH2503 |
| D | HOH2581 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL D 2310 |
| Chain | Residue |
| D | ASP104 |
| D | LEU106 |
| D | GLY181 |
| D | GLN182 |
| D | HOH2467 |
| D | HOH2544 |
| D | PRO96 |
| D | CYS99 |
| D | ALA100 |
| D | ASN103 |
| site_id | BC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL A 2311 |
| Chain | Residue |
| A | PRO96 |
| A | CYS99 |
| A | ALA100 |
| A | ASN103 |
| A | ASP104 |
| A | LEU106 |
| A | GLY181 |
| A | GLN182 |
| A | VAL183 |
| A | HOH2468 |
| A | HOH2675 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 2312 |
| Chain | Residue |
| B | HIS126 |
| B | ASP127 |
| B | ASP156 |
| B | HOH2400 |
| B | HOH2573 |
| B | HOH2621 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 2313 |
| Chain | Residue |
| A | HIS126 |
| A | ASP127 |
| A | ASN152 |
| A | ASP156 |
| A | HOH2377 |
| A | HOH2516 |
| A | HOH2678 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL C 2314 |
| Chain | Residue |
| C | GLU310 |
| C | HOH2511 |
| C | HOH2608 |
| D | ARG120 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 2315 |
| Chain | Residue |
| C | ASP48 |
| C | ALA266 |
| C | HOH2323 |
| C | HOH2591 |
| D | MET202 |
| D | MET207 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17320106","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22360758","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"17320106","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22360758","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 48 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17320106","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22360758","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xvt |
| Chain | Residue | Details |
| A | ASP156 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xvt |
| Chain | Residue | Details |
| B | ASP156 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xvt |
| Chain | Residue | Details |
| C | ASP156 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xvt |
| Chain | Residue | Details |
| D | ASP156 |
