6COM
2.3A crystal structure of E. coli phosphoenolpyruvate carboxykinase mutant Asp269Asn
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004611 | molecular_function | phosphoenolpyruvate carboxykinase activity |
| A | 0004612 | molecular_function | phosphoenolpyruvate carboxykinase (ATP) activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0017076 | molecular_function | purine nucleotide binding |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | binding site for residue ATP A 601 |
| Chain | Residue |
| A | LEU249 |
| A | TYR286 |
| A | LYS288 |
| A | GLU297 |
| A | ARG333 |
| A | ARG449 |
| A | ILE450 |
| A | SER451 |
| A | ILE452 |
| A | THR455 |
| A | PYR602 |
| A | SER250 |
| A | CA603 |
| A | MG604 |
| A | HOH704 |
| A | HOH708 |
| A | HOH733 |
| A | HOH744 |
| A | GLY251 |
| A | THR252 |
| A | GLY253 |
| A | LYS254 |
| A | THR255 |
| A | THR256 |
| A | ASN269 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue PYR A 602 |
| Chain | Residue |
| A | ARG65 |
| A | TYR207 |
| A | LYS213 |
| A | ARG333 |
| A | ATP601 |
| A | CA603 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 603 |
| Chain | Residue |
| A | HIS232 |
| A | ATP601 |
| A | PYR602 |
| A | HOH704 |
| A | HOH708 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue MG A 604 |
| Chain | Residue |
| A | THR255 |
| A | TYR286 |
| A | ATP601 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00453","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11724534","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00453","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of E. coli phosphoenolpyruvate carboxykinase mutant Lys213Ser.","authors":["Delbaere L.T.J.","Cotelesage J.J.H.","Goldie H."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00453","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12837799","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17475535","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8599762","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9406547","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of E. coli phosphoenolpyruvate carboxykinase (PEPCK) complexed with ATP, Mg2+, Mn2+, carbon dioxide and oxaloacetate.","authors":["Delbaere L.T.J.","Cotelesage J.J.H.","Goldie H."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of E. coli phosphoenolpyruvate carboxykinase mutant Lys213Ser.","authors":["Delbaere L.T.J.","Cotelesage J.J.H.","Goldie H."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"HAMAP-Rule","id":"MF_00453","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 51 |
| Chain | Residue | Details |
| A | ARG65 | electrostatic stabiliser, increase electrophilicity |
| A | LYS213 | metal ligand |
| A | HIS232 | electrostatic stabiliser, hydrogen bond donor, metal ligand |
| A | SER250 | steric role |
| A | LYS254 | electrostatic stabiliser, hydrogen bond donor |
| A | THR255 | metal ligand |
| A | ASN269 | metal ligand |
| A | ARG333 | electrostatic stabiliser, hydrogen bond donor |
