3MOE
The structure of rat cytosolic PEPCK mutant A467G in complex with Beta-Sulfopyruvate and GTP
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 | 34 |
| Details | BINDING SITE FOR RESIDUE GTP A 1100 |
| Chain | Residue |
| A | HIS264 |
| A | ASP311 |
| A | VAL335 |
| A | ARG405 |
| A | ARG436 |
| A | TRP516 |
| A | PHE517 |
| A | PHE525 |
| A | GLY529 |
| A | PHE530 |
| A | ASN533 |
| A | PRO285 |
| A | HOH641 |
| A | HOH647 |
| A | HOH684 |
| A | MN700 |
| A | MN701 |
| A | HOH716 |
| A | HOH720 |
| A | HOH723 |
| A | HOH760 |
| A | HOH825 |
| A | SER286 |
| A | HOH826 |
| A | HOH917 |
| A | HOH994 |
| A | HOH1053 |
| A | SPV1200 |
| A | ALA287 |
| A | CYS288 |
| A | GLY289 |
| A | LYS290 |
| A | THR291 |
| A | ASN292 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 700 |
| Chain | Residue |
| A | LYS244 |
| A | HIS264 |
| A | ASP311 |
| A | GTP1100 |
| A | SPV1200 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 701 |
| Chain | Residue |
| A | THR291 |
| A | HOH684 |
| A | HOH712 |
| A | HOH716 |
| A | GTP1100 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 800 |
| Chain | Residue |
| A | LEU79 |
| A | ASN208 |
| A | HOH769 |
| A | HOH772 |
| A | HOH787 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE SPV A 1200 |
| Chain | Residue |
| A | ARG87 |
| A | GLY237 |
| A | LYS243 |
| A | LYS244 |
| A | HIS264 |
| A | SER286 |
| A | ASP311 |
| A | PHE333 |
| A | ARG405 |
| A | HOH636 |
| A | HOH663 |
| A | MN700 |
| A | HOH765 |
| A | GTP1100 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 1PE A 1300 |
| Chain | Residue |
| A | ASN7 |
| A | GLY8 |
| A | ASP10 |
| A | PHE11 |
| A | LYS14 |
| A | HOH1179 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 1PE A 1301 |
| Chain | Residue |
| A | ALA447 |
| A | SER449 |
| A | LEU508 |
| A | PRO509 |
| A | LYS510 |
| A | ILE511 |
| A | HOH1105 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE 1PE A 1302 |
| Chain | Residue |
| A | ALA128 |
| A | PRO131 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 1400 |
| Chain | Residue |
| A | ARG543 |
| A | HOH1129 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 1401 |
| Chain | Residue |
| A | LYS155 |
| A | ILE156 |
| A | GLU188 |
| A | HOH837 |
| A | HOH1111 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 1402 |
| Chain | Residue |
| A | SER411 |
| A | CYS413 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1403 |
| Chain | Residue |
| A | GLU274 |
| A | ARG437 |
| A | ALA439 |
| A | ILE475 |
| A | HOH650 |
| A | HOH1119 |
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 |
