2RKE
The Structure of rat cytosolic PEPCK in complex with sulfoacetate.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004550 | molecular_function | nucleoside diphosphate kinase activity |
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 | 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 | 0014823 | biological_process | response to activity |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0016831 | molecular_function | carboxy-lyase activity |
A | 0017076 | molecular_function | purine nucleotide binding |
A | 0018105 | biological_process | peptidyl-serine phosphorylation |
A | 0019003 | molecular_function | GDP binding |
A | 0019543 | biological_process | propionate catabolic process |
A | 0030145 | molecular_function | manganese ion binding |
A | 0031406 | molecular_function | carboxylic acid binding |
A | 0031667 | biological_process | response to nutrient levels |
A | 0032496 | biological_process | response to lipopolysaccharide |
A | 0032868 | biological_process | response to insulin |
A | 0032869 | biological_process | cellular response to insulin stimulus |
A | 0033993 | biological_process | response to lipid |
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 | 0070365 | biological_process | hepatocyte differentiation |
A | 0070741 | biological_process | response to interleukin-6 |
A | 0071300 | biological_process | cellular response to retinoic acid |
A | 0071320 | biological_process | cellular response to cAMP |
A | 0071332 | biological_process | cellular response to fructose stimulus |
A | 0071333 | biological_process | cellular response to glucose stimulus |
A | 0071347 | biological_process | cellular response to interleukin-1 |
A | 0071356 | biological_process | cellular response to tumor necrosis factor |
A | 0071377 | biological_process | cellular response to glucagon stimulus |
A | 0071456 | biological_process | cellular response to hypoxia |
A | 0071474 | biological_process | cellular hyperosmotic response |
A | 0071475 | biological_process | cellular hyperosmotic salinity response |
A | 0071476 | biological_process | cellular hypotonic response |
A | 0071477 | biological_process | cellular hypotonic salinity response |
A | 0071549 | biological_process | cellular response to dexamethasone stimulus |
A | 0072350 | biological_process | tricarboxylic acid metabolic process |
A | 0097403 | biological_process | cellular response to raffinose |
A | 0106264 | molecular_function | protein serine kinase activity (using GTP as donor) |
A | 1904628 | biological_process | cellular response to phorbol 13-acetate 12-myristate |
A | 1904640 | biological_process | response to methionine |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 700 |
Chain | Residue |
A | LYS244 |
A | HIS264 |
A | ASP311 |
A | HOH842 |
A | HOH844 |
A | HOH863 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MN A 701 |
Chain | Residue |
A | HIS502 |
A | GLU607 |
A | HOH1132 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 702 |
Chain | Residue |
A | LEU79 |
A | ASN208 |
A | HOH751 |
A | HOH1037 |
A | HOH1065 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 703 |
Chain | Residue |
A | GLY289 |
A | LYS290 |
A | THR291 |
A | HOH783 |
A | HOH910 |
A | HOH914 |
A | HOH938 |
A | HOH957 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SAT A 704 |
Chain | Residue |
A | ALA86 |
A | ARG87 |
A | TYR235 |
A | GLY237 |
A | LYS243 |
A | LYS244 |
A | ASN403 |
A | HOH844 |
A | HOH1116 |
A | HOH1135 |
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 | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:23127136, ECO:0000269|PubMed:2909519 |
Chain | Residue | Details |
A | CYS288 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17685635, ECO:0000269|PubMed:18772387, ECO:0000269|PubMed:20476774, ECO:0000269|PubMed:23127136, ECO:0000269|PubMed:24863970 |
Chain | Residue | Details |
A | ARG87 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18197707, ECO:0000269|PubMed:18772387, ECO:0000269|PubMed:20476774, ECO:0000269|PubMed:23127136, ECO:0000269|PubMed:24863970 |
Chain | Residue | Details |
A | TYR235 | |
A | ASN403 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17685635, ECO:0000269|PubMed:18197707, ECO:0000269|PubMed:18772387, ECO:0000269|PubMed:20476774, ECO:0000269|PubMed:23127136, ECO:0000269|PubMed:24863970, ECO:0000269|PubMed:26322521, ECO:0000269|PubMed:26709450, ECO:0000269|PubMed:28345895, ECO:0000269|PubMed:31461616, ECO:0007744|PDB:4YW9, ECO:0007744|PDB:5FH0, ECO:0007744|PDB:5FH1, ECO:0007744|PDB:5FH2, ECO:0007744|PDB:5FH3, ECO:0007744|PDB:5FH4, ECO:0007744|PDB:5FH5, ECO:0007744|PDB:5V97, ECO:0007744|PDB:5V9F, ECO:0007744|PDB:5V9G, ECO:0007744|PDB:6P5O |
Chain | Residue | Details |
A | LYS244 | |
A | HIS264 | |
A | ASP311 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17685635, ECO:0000269|PubMed:18197707, ECO:0000269|PubMed:18772387, ECO:0000269|PubMed:20476774, ECO:0000269|PubMed:23127136, ECO:0000269|PubMed:24863970 |
Chain | Residue | Details |
A | SER286 |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17685635, ECO:0000269|PubMed:18772387, ECO:0000269|PubMed:20476774, ECO:0000269|PubMed:23127136, ECO:0000269|PubMed:24863970, ECO:0000269|PubMed:26322521, ECO:0000269|PubMed:26709450, ECO:0000269|PubMed:28345895, ECO:0007744|PDB:4YW9, ECO:0007744|PDB:5FH0, ECO:0007744|PDB:5FH1, ECO:0007744|PDB:5FH2, ECO:0007744|PDB:5FH3, ECO:0007744|PDB:5FH4, ECO:0007744|PDB:5V97, ECO:0007744|PDB:5V9F, ECO:0007744|PDB:5V9G |
Chain | Residue | Details |
A | ALA287 | |
A | ARG436 | |
A | PHE530 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17685635, ECO:0000269|PubMed:20476774, ECO:0000269|PubMed:23127136, ECO:0000269|PubMed:24863970, ECO:0000269|PubMed:26322521, ECO:0000269|PubMed:26709450, ECO:0000269|PubMed:28345895, ECO:0007744|PDB:4YW9, ECO:0007744|PDB:5FH0, ECO:0007744|PDB:5FH1, ECO:0007744|PDB:5FH2, ECO:0007744|PDB:5FH3, ECO:0007744|PDB:5FH4, ECO:0007744|PDB:5V97, ECO:0007744|PDB:5V9F, ECO:0007744|PDB:5V9G |
Chain | Residue | Details |
A | ARG405 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
Chain | Residue | Details |
A | SER19 | |
A | SER118 |
site_id | SWS_FT_FI9 |
Number of Residues | 3 |
Details | MOD_RES: N6-acetyllysine; by p300/EP300 => ECO:0000250|UniProtKB:P35558 |
Chain | Residue | Details |
A | LYS70 | |
A | LYS71 | |
A | LYS594 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P35558 |
Chain | Residue | Details |
A | SER90 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine; by p300/EP300 => ECO:0000250|UniProtKB:P35558, ECO:0000269|PubMed:30193097 |
Chain | Residue | Details |
A | LYS91 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q16822 |
Chain | Residue | Details |
A | THR178 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q16822 |
Chain | Residue | Details |
A | SER286 |
site_id | SWS_FT_FI14 |
Number of Residues | 3 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:30193097 |
Chain | Residue | Details |
A | LYS473 | |
A | LYS521 | |
A | LYS524 |
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 |