4WPU
Crystal Structure of E83A mutant of Mtb PEPCK in complex with PEP and GDP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004611 | molecular_function | phosphoenolpyruvate carboxykinase activity |
| A | 0004613 | molecular_function | phosphoenolpyruvate carboxykinase (GTP) activity |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0006107 | biological_process | oxaloacetate metabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0017076 | molecular_function | purine nucleotide binding |
| A | 0019543 | biological_process | propionate catabolic process |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0033993 | biological_process | response to lipid |
| A | 0042594 | biological_process | response to starvation |
| A | 0046327 | biological_process | glycerol biosynthetic process from pyruvate |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071333 | biological_process | cellular response to glucose stimulus |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue GDP A 701 |
| Chain | Residue |
| A | PRO270 |
| A | TRP501 |
| A | PHE502 |
| A | PHE510 |
| A | GLY514 |
| A | PHE515 |
| A | ASN518 |
| A | HOH817 |
| A | HOH876 |
| A | HOH1089 |
| A | ALA272 |
| A | CYS273 |
| A | GLY274 |
| A | LYS275 |
| A | THR276 |
| A | ASN277 |
| A | ASP362 |
| A | ARG420 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 702 |
| Chain | Residue |
| A | THR86 |
| A | ILE88 |
| A | THR99 |
| A | ASN100 |
| A | ASN101 |
| A | ARG234 |
| A | LEU467 |
| A | PRO468 |
| A | HOH1052 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue PEP A 703 |
| Chain | Residue |
| A | ARG81 |
| A | GLY221 |
| A | GLY222 |
| A | ARG389 |
| A | HOH962 |
Functional Information from PROSITE/UniProt
| site_id | PS00505 |
| Number of Residues | 9 |
| Details | PEPCK_GTP Phosphoenolpyruvate carboxykinase (GTP) signature. FPSACGKTN |
| Chain | Residue | Details |
| A | PHE269-ASN277 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P07379","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00452","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00452","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2014","submissionDatabase":"PDB data bank","title":"Crystal Structure of PEPCK (Rv0211) from Mycobacterium tuberculosis in complex with oxalate and Mn2+.","authors":["Kim H.L.","Sacchettini J.C."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 13 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P07379","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00452","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
