1KHF
PEPCK complex with PEP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion 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 | 0005739 | cellular_component | mitochondrion |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005829 | cellular_component | cytosol |
| A | 0006006 | biological_process | glucose metabolic process |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0006107 | biological_process | oxaloacetate metabolic process |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0009617 | biological_process | response to bacterium |
| A | 0010447 | biological_process | response to acidic pH |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0017076 | molecular_function | purine nucleotide binding |
| A | 0018105 | biological_process | peptidyl-serine phosphorylation |
| A | 0019543 | biological_process | propionate catabolic process |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0031406 | molecular_function | carboxylic acid binding |
| A | 0032868 | biological_process | response to insulin |
| A | 0032869 | biological_process | cellular response to insulin stimulus |
| A | 0042593 | biological_process | glucose homeostasis |
| A | 0042594 | biological_process | response to starvation |
| A | 0043382 | biological_process | positive regulation of memory T cell differentiation |
| A | 0043648 | biological_process | dicarboxylic acid metabolic process |
| A | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| A | 0046166 | biological_process | glyceraldehyde-3-phosphate biosynthetic process |
| A | 0046327 | biological_process | glycerol biosynthetic process from pyruvate |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046889 | biological_process | positive regulation of lipid biosynthetic process |
| A | 0046890 | biological_process | regulation of lipid biosynthetic process |
| A | 0051365 | biological_process | cellular response to potassium ion starvation |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0070365 | biological_process | hepatocyte differentiation |
| A | 0071333 | biological_process | cellular response to glucose stimulus |
| A | 0071549 | biological_process | cellular response to dexamethasone stimulus |
| A | 0072350 | biological_process | tricarboxylic acid metabolic process |
| A | 0106264 | molecular_function | protein serine kinase activity (using GTP as donor) |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 701 |
| Chain | Residue |
| A | LYS244 |
| A | HIS264 |
| A | ASP311 |
| A | HOH732 |
| A | HOH797 |
| A | HOH804 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 702 |
| Chain | Residue |
| A | PEP703 |
| A | HOH813 |
| A | HOH861 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PEP A 703 |
| Chain | Residue |
| A | ALA86 |
| A | ARG87 |
| A | TYR235 |
| A | GLY236 |
| A | GLY237 |
| A | LYS244 |
| A | ASN403 |
| A | ARG405 |
| A | NA702 |
| A | HOH732 |
| A | HOH797 |
| A | HOH819 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 704 |
| Chain | Residue |
| A | TRP450 |
| A | PRO509 |
| A | LYS510 |
| A | ILE511 |
| A | HOH824 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 705 |
| Chain | Residue |
| A | TYR72 |
| A | GLN352 |
| A | VAL368 |
| A | ILE373 |
| A | HOH746 |
Functional Information from PROSITE/UniProt
| site_id | PS00505 |
| Number of Residues | 9 |
| Details | PEPCK_GTP Phosphoenolpyruvate carboxykinase (GTP) signature. FPSACGKTN |
| Chain | Residue | Details |
| A | PHE284-ASN292 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"11851336","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32322062","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11851336","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14552798","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17532214","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P07379","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11851336","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine; by p300/EP300","evidences":[{"source":"PubMed","id":"20167786","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21726808","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by PKB/AKT1","evidences":[{"source":"PubMed","id":"32322062","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine; by p300/EP300","evidences":[{"source":"PubMed","id":"30193097","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9Z2V4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q16822","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q16822","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P07379","evidenceCode":"ECO:0000250"}]} |
| 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 | HIS264 | |
| A | LYS290 | |
| A | ARG405 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1aq2 |
| Chain | Residue | Details |
| A | HIS264 | |
| A | ARG405 |
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 863 |
| Chain | Residue | Details |
| A | ARG87 | electrostatic stabiliser, enhance reactivity |
| A | TYR235 | electrostatic stabiliser, steric role |
| A | LYS244 | metal ligand |
| A | HIS264 | metal ligand |
| A | SER286 | electrostatic stabiliser |
| A | CYS288 | metal ligand |
| A | ASP311 | metal ligand |
| A | ARG405 | electrostatic stabiliser, enhance reactivity |
