1U0E
Crystal structure of mouse phosphoglucose isomerase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0002639 | biological_process | positive regulation of immunoglobulin production |
| A | 0004347 | molecular_function | glucose-6-phosphate isomerase activity |
| A | 0005125 | molecular_function | cytokine activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0006096 | biological_process | glycolytic process |
| A | 0007165 | biological_process | signal transduction |
| A | 0007611 | biological_process | learning or memory |
| A | 0008083 | molecular_function | growth factor activity |
| A | 0010595 | biological_process | positive regulation of endothelial cell migration |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016857 | molecular_function | racemase and epimerase activity, acting on carbohydrates and derivatives |
| A | 0031625 | molecular_function | ubiquitin protein ligase binding |
| A | 0032355 | biological_process | response to estradiol |
| A | 0032570 | biological_process | response to progesterone |
| A | 0033574 | biological_process | response to testosterone |
| A | 0035902 | biological_process | response to immobilization stress |
| A | 0035994 | biological_process | response to muscle stretch |
| A | 0043066 | biological_process | negative regulation of apoptotic process |
| A | 0043209 | cellular_component | myelin sheath |
| A | 0046686 | biological_process | response to cadmium ion |
| A | 0047938 | molecular_function | glucose-6-phosphate 1-epimerase activity |
| A | 0048029 | molecular_function | monosaccharide binding |
| A | 0051156 | biological_process | glucose 6-phosphate metabolic process |
| A | 0097367 | molecular_function | carbohydrate derivative binding |
| A | 1901135 | biological_process | carbohydrate derivative metabolic process |
| B | 0002639 | biological_process | positive regulation of immunoglobulin production |
| B | 0004347 | molecular_function | glucose-6-phosphate isomerase activity |
| B | 0005125 | molecular_function | cytokine activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| B | 0006094 | biological_process | gluconeogenesis |
| B | 0006096 | biological_process | glycolytic process |
| B | 0007165 | biological_process | signal transduction |
| B | 0007611 | biological_process | learning or memory |
| B | 0008083 | molecular_function | growth factor activity |
| B | 0010595 | biological_process | positive regulation of endothelial cell migration |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016857 | molecular_function | racemase and epimerase activity, acting on carbohydrates and derivatives |
| B | 0031625 | molecular_function | ubiquitin protein ligase binding |
| B | 0032355 | biological_process | response to estradiol |
| B | 0032570 | biological_process | response to progesterone |
| B | 0033574 | biological_process | response to testosterone |
| B | 0035902 | biological_process | response to immobilization stress |
| B | 0035994 | biological_process | response to muscle stretch |
| B | 0043066 | biological_process | negative regulation of apoptotic process |
| B | 0043209 | cellular_component | myelin sheath |
| B | 0046686 | biological_process | response to cadmium ion |
| B | 0047938 | molecular_function | glucose-6-phosphate 1-epimerase activity |
| B | 0048029 | molecular_function | monosaccharide binding |
| B | 0051156 | biological_process | glucose 6-phosphate metabolic process |
| B | 0097367 | molecular_function | carbohydrate derivative binding |
| B | 1901135 | biological_process | carbohydrate derivative metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1201 |
| Chain | Residue |
| A | SER159 |
| A | SER209 |
| A | LYS210 |
| A | THR211 |
| A | THR214 |
| A | HOH1259 |
| A | HOH1479 |
| A | HOH1638 |
| A | HOH1739 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1202 |
| Chain | Residue |
| A | ALA1 |
| A | ALA2 |
| A | ARG5 |
| A | SER366 |
| A | ALA368 |
| A | HOH1364 |
| A | HOH1442 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1203 |
| Chain | Residue |
| B | ARG136 |
| B | HOH1279 |
| B | HOH1513 |
| B | HOH1612 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1204 |
| Chain | Residue |
| B | ALA368 |
| B | ARG369 |
| B | HOH1613 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1205 |
| Chain | Residue |
| B | GLY158 |
| B | GLY271 |
| B | ARG272 |
| B | GLN353 |
| B | HOH1366 |
| B | HOH1544 |
| B | HOH1704 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1206 |
| Chain | Residue |
| A | ASN46 |
| A | HIS47 |
| A | HOH1527 |
| A | HOH1745 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1207 |
| Chain | Residue |
| A | ARG105 |
| A | SER297 |
| A | HOH1526 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1208 |
| Chain | Residue |
| B | LYS146 |
| B | SER147 |
| B | HOH1283 |
| B | HOH1375 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1209 |
| Chain | Residue |
| B | THR211 |
| B | THR213 |
| B | THR214 |
| B | HOH1448 |
| B | HOH1490 |
| B | HOH1645 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1210 |
| Chain | Residue |
| A | LYS522 |
| A | HOH1595 |
| B | GLY530 |
| B | SER531 |
| B | SER532 |
| B | HOH1552 |
| B | HOH1624 |
| B | HOH1641 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME A 1211 |
| Chain | Residue |
| A | GLY418 |
| A | HOH1353 |
| A | HOH1438 |
| B | ARG552 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME A 1212 |
| Chain | Residue |
| A | ARG346 |
| A | GOL1225 |
| A | HOH1640 |
| B | GLN342 |
| B | HOH1352 |
| B | HOH1511 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME A 1213 |
| Chain | Residue |
| A | HIS49 |
| B | GLN551 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME A 1214 |
| Chain | Residue |
| A | THR149 |
| A | ARG179 |
| A | HOH1545 |
| A | HOH1716 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME A 1215 |
| Chain | Residue |
| A | LEU195 |
| A | LEU198 |
| A | TRP227 |
| A | HOH1451 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1221 |
| Chain | Residue |
| A | ARG134 |
| A | ASP139 |
| A | TRP140 |
| A | LYS141 |
| A | LYS240 |
| A | HOH1569 |
| A | HOH1616 |
| A | HOH1625 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1222 |
| Chain | Residue |
| B | GLN8 |
| B | SER73 |
| B | HOH1505 |
| B | HOH1534 |
| B | HOH1536 |
| site_id | BC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 1223 |
| Chain | Residue |
| A | ASN470 |
| A | ARG471 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1224 |
| Chain | Residue |
| B | ASN38 |
| B | TYR54 |
| B | LYS61 |
| B | MET64 |
| B | HOH1321 |
| B | HOH1498 |
| site_id | CC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1225 |
| Chain | Residue |
| A | BME1212 |
| A | HOH1446 |
| A | HOH1536 |
| A | HOH1639 |
| A | GLU168 |
| A | PHE182 |
| A | HIS345 |
| site_id | CC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1226 |
| Chain | Residue |
| A | PHE131 |
| A | VAL243 |
| A | GLN260 |
| A | ASN261 |
| A | LEU263 |
| A | HOH1443 |
| A | HOH1624 |
| site_id | CC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 1227 |
| Chain | Residue |
| A | LYS171 |
| A | ARG179 |
| A | VAL180 |
| A | HIS286 |
| A | HOH1400 |
| A | HOH1529 |
| A | HOH1581 |
| A | HOH1608 |
| A | HOH1637 |
Functional Information from PROSITE/UniProt
| site_id | PS00174 |
| Number of Residues | 18 |
| Details | P_GLUCOSE_ISOMERASE_2 Phosphoglucose isomerase signature 2. GiMWdinsFDQwGVElgK |
| Chain | Residue | Details |
| A | GLY501-LYS518 |
| site_id | PS00765 |
| Number of Residues | 14 |
| Details | P_GLUCOSE_ISOMERASE_1 Phosphoglucose isomerase signature 1. DwVGGRYSLwSAIG |
| Chain | Residue | Details |
| A | ASP267-GLY280 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"15342241","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"15342241","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15342241","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16375918","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1U0F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CXS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CXT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q6P6V0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by CK2","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q6P6V0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1dqr |
| Chain | Residue | Details |
| A | HIS388 | |
| B | ARG272 | |
| B | LYS518 | |
| B | GLU216 | |
| B | GLU357 | |
| B | LYS210 | |
| B | GLY271 |
| site_id | CSA2 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1dqr |
| Chain | Residue | Details |
| A | ARG272 | |
| A | LYS518 | |
| A | GLU216 | |
| A | GLU357 | |
| A | LYS210 | |
| A | GLY271 | |
| B | HIS388 |
