1U0G
Crystal structure of mouse phosphoglucose isomerase in complex with erythrose 4-phosphate
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 | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 951 |
| Chain | Residue |
| A | ALA1 |
| A | ALA2 |
| A | ARG5 |
| A | SER366 |
| A | ALA368 |
| A | HOH1102 |
| A | HOH1305 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 952 |
| Chain | Residue |
| B | HOH1287 |
| B | ARG136 |
| B | HOH1199 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 953 |
| Chain | Residue |
| B | ALA368 |
| B | ARG369 |
| B | HOH1226 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 954 |
| Chain | Residue |
| A | ARG105 |
| A | SER297 |
| A | HOH1367 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 955 |
| Chain | Residue |
| B | LYS146 |
| B | SER147 |
| B | HOH1029 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 956 |
| Chain | Residue |
| A | THR149 |
| A | ARG179 |
| A | HOH1287 |
| A | HOH1361 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 957 |
| Chain | Residue |
| B | ARG179 |
| B | HOH1317 |
| site_id | AC8 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE E4P A 901 |
| Chain | Residue |
| A | ILE156 |
| A | GLY157 |
| A | GLY158 |
| A | SER159 |
| A | SER209 |
| A | LYS210 |
| A | THR211 |
| A | THR214 |
| A | GLN353 |
| A | GLU357 |
| A | LYS518 |
| A | HOH1004 |
| A | HOH1007 |
| A | HOH1225 |
| A | HOH1242 |
| A | HOH1247 |
| B | HIS388 |
| site_id | AC9 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE E4P B 902 |
| Chain | Residue |
| A | HIS388 |
| B | ILE156 |
| B | GLY157 |
| B | GLY158 |
| B | SER159 |
| B | SER209 |
| B | LYS210 |
| B | THR211 |
| B | THR214 |
| B | GLN353 |
| B | GLU357 |
| B | HOH1059 |
| B | HOH1152 |
| B | HOH1161 |
| B | HOH1214 |
| B | HOH1215 |
| B | HOH1216 |
| B | HOH1217 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME B 961 |
| Chain | Residue |
| A | GLY418 |
| A | LYS422 |
| A | HOH1093 |
| A | HOH1153 |
| B | ARG552 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME A 962 |
| Chain | Residue |
| A | ARG346 |
| B | GLN342 |
| B | HIS345 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME A 963 |
| Chain | Residue |
| A | LEU41 |
| A | ASN42 |
| A | HOH1117 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BME A 964 |
| Chain | Residue |
| A | PRO463 |
| A | VAL466 |
| A | GLU468 |
| A | HOH1333 |
| B | TYR362 |
| B | ILE363 |
| B | ARG369 |
| B | HOH1309 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME B 966 |
| Chain | Residue |
| B | ASN82 |
| B | SER87 |
| B | ILE89 |
| B | HOH1394 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 971 |
| Chain | Residue |
| A | ARG134 |
| A | ASP139 |
| A | TRP140 |
| A | LYS141 |
| A | LYS240 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 972 |
| Chain | Residue |
| B | PRO7 |
| B | GLN8 |
| B | SER73 |
| B | HOH1197 |
| B | HOH1208 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 973 |
| Chain | Residue |
| A | ARG105 |
| A | ASN122 |
| A | LEU125 |
| A | ASP126 |
| A | GLU293 |
| A | HOH1198 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 974 |
| Chain | Residue |
| A | THR223 |
| A | TRP227 |
| A | HOH1105 |
| A | HOH1228 |
| A | HOH1231 |
| site_id | CC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 975 |
| Chain | Residue |
| A | ASN104 |
| A | SER106 |
| A | THR108 |
| A | GLN304 |
| A | LEU307 |
| A | HOH1170 |
| A | HOH1221 |
| A | HOH1350 |
| A | HOH1375 |
| site_id | CC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 976 |
| Chain | Residue |
| A | LYS127 |
| A | PHE131 |
| A | VAL243 |
| A | GLN260 |
| A | ASN261 |
| A | LEU263 |
| A | HOH1156 |
| A | HOH1226 |
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 |
