2GMV
PEPCK complex with a GTP-competitive inhibitor
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) |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004611 | molecular_function | phosphoenolpyruvate carboxykinase activity |
| B | 0004613 | molecular_function | phosphoenolpyruvate carboxykinase (GTP) activity |
| B | 0005525 | molecular_function | GTP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005829 | cellular_component | cytosol |
| B | 0006006 | biological_process | glucose metabolic process |
| B | 0006094 | biological_process | gluconeogenesis |
| B | 0006107 | biological_process | oxaloacetate metabolic process |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0009617 | biological_process | response to bacterium |
| B | 0010447 | biological_process | response to acidic pH |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0017076 | molecular_function | purine nucleotide binding |
| B | 0018105 | biological_process | peptidyl-serine phosphorylation |
| B | 0019543 | biological_process | propionate catabolic process |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0031406 | molecular_function | carboxylic acid binding |
| B | 0032868 | biological_process | response to insulin |
| B | 0032869 | biological_process | cellular response to insulin stimulus |
| B | 0042593 | biological_process | glucose homeostasis |
| B | 0042594 | biological_process | response to starvation |
| B | 0043382 | biological_process | positive regulation of memory T cell differentiation |
| B | 0043648 | biological_process | dicarboxylic acid metabolic process |
| B | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| B | 0046166 | biological_process | glyceraldehyde-3-phosphate biosynthetic process |
| B | 0046327 | biological_process | glycerol biosynthetic process from pyruvate |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0046889 | biological_process | positive regulation of lipid biosynthetic process |
| B | 0046890 | biological_process | regulation of lipid biosynthetic process |
| B | 0051365 | biological_process | cellular response to potassium ion starvation |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0070365 | biological_process | hepatocyte differentiation |
| B | 0071333 | biological_process | cellular response to glucose stimulus |
| B | 0071549 | biological_process | cellular response to dexamethasone stimulus |
| B | 0072350 | biological_process | tricarboxylic acid metabolic process |
| B | 0106264 | molecular_function | protein serine kinase activity (using GTP as donor) |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN A 701 |
| Chain | Residue |
| A | LYS244 |
| A | HIS264 |
| A | ASP311 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN B 701 |
| Chain | Residue |
| B | LYS244 |
| B | HIS264 |
| B | ASP311 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PEP A 702 |
| Chain | Residue |
| A | GLY236 |
| A | GLY237 |
| A | LYS244 |
| A | ASN403 |
| A | ARG405 |
| A | HOH776 |
| A | ALA86 |
| A | ARG87 |
| A | TYR235 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PEP B 702 |
| Chain | Residue |
| B | ALA86 |
| B | ARG87 |
| B | TYR235 |
| B | GLY236 |
| B | GLY237 |
| B | LYS244 |
| B | ASN403 |
| B | ARG405 |
| B | PHE485 |
| B | HOH715 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE UN8 A 703 |
| Chain | Residue |
| A | ALA287 |
| A | CYS288 |
| A | GLY289 |
| A | ASN292 |
| A | LEU293 |
| A | THR343 |
| A | TRP516 |
| A | PHE517 |
| A | PHE525 |
| A | TRP527 |
| A | PHE530 |
| A | ASN533 |
| A | HOH740 |
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 | 2 |
| 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 | 22 |
| 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 | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P07379","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11851336","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| 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 | 2 |
| 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 | 2 |
| 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 | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9Z2V4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q16822","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q16822","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P07379","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| 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 |
| site_id | MCSA2 |
| Number of Residues | 8 |
| Details | M-CSA 863 |
| Chain | Residue | Details |
| B | ARG87 | electrostatic stabiliser, enhance reactivity |
| B | TYR235 | electrostatic stabiliser, steric role |
| B | LYS244 | metal ligand |
| B | HIS264 | metal ligand |
| B | SER286 | electrostatic stabiliser |
| B | CYS288 | metal ligand |
| B | ASP311 | metal ligand |
| B | ARG405 | electrostatic stabiliser, enhance reactivity |
| 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 | 3 |
| Details | Annotated By Reference To The Literature 1aq2 |
| Chain | Residue | Details |
| B | HIS264 | |
| B | LYS290 | |
| B | ARG405 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1aq2 |
| Chain | Residue | Details |
| A | HIS264 | |
| A | ARG405 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1aq2 |
| Chain | Residue | Details |
| B | HIS264 | |
| B | ARG405 |
