1OS1
Structure of Phosphoenolpyruvate Carboxykinase complexed with ATP,Mg, Ca and pyruvate.
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 | 7 |
Details | BINDING SITE FOR RESIDUE MG A 998 |
Chain | Residue |
A | THR255 |
A | ASP268 |
A | TYR286 |
A | ATP541 |
A | HOH674 |
A | HOH716 |
A | HOH738 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 999 |
Chain | Residue |
A | ASP269 |
A | ATP541 |
A | PYR542 |
A | HOH719 |
A | LYS213 |
A | HIS232 |
site_id | AC3 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE ATP A 541 |
Chain | Residue |
A | LEU249 |
A | SER250 |
A | GLY251 |
A | THR252 |
A | GLY253 |
A | LYS254 |
A | THR255 |
A | THR256 |
A | ASP269 |
A | ARG333 |
A | ARG449 |
A | ILE450 |
A | SER451 |
A | ILE452 |
A | THR455 |
A | HOH674 |
A | HOH716 |
A | HOH719 |
A | HOH738 |
A | HOH754 |
A | MG998 |
A | CA999 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PYR A 542 |
Chain | Residue |
A | ARG65 |
A | TYR207 |
A | LYS213 |
A | SER250 |
A | GLY393 |
A | CA999 |
Functional Information from PROSITE/UniProt
site_id | PS00532 |
Number of Residues | 16 |
Details | PEPCK_ATP Phosphoenolpyruvate carboxykinase (ATP) signature. LIGDDEHgWdDdGVfN |
Chain | Residue | Details |
A | LEU265-ASN280 |
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 | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1aq2 |
Chain | Residue | Details |
A | LYS254 | |
A | ARG333 | |
A | HIS232 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1aq2 |
Chain | Residue | Details |
A | ARG333 | |
A | HIS232 |
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 | ASP269 | metal ligand |
A | ARG333 | electrostatic stabiliser, hydrogen bond donor |