1XTB
Crystal Structure of Rabbit Phosphoglucose Isomerase Complexed with Sorbitol-6-Phosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004347 | molecular_function | glucose-6-phosphate isomerase activity |
| A | 0005125 | molecular_function | cytokine activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0006096 | biological_process | glycolytic process |
| A | 0007165 | biological_process | signal transduction |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016857 | molecular_function | racemase and epimerase activity, acting on carbohydrates and derivatives |
| 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 | 0004347 | molecular_function | glucose-6-phosphate isomerase activity |
| B | 0005125 | molecular_function | cytokine activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006094 | biological_process | gluconeogenesis |
| B | 0006096 | biological_process | glycolytic process |
| B | 0007165 | biological_process | signal transduction |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016857 | molecular_function | racemase and epimerase activity, acting on carbohydrates and derivatives |
| 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 | 18 |
| Details | BINDING SITE FOR RESIDUE S6P A 2002 |
| Chain | Residue |
| A | GLY157 |
| A | GLN353 |
| A | GLU357 |
| A | GLN511 |
| A | HOH3067 |
| A | HOH3129 |
| A | HOH3215 |
| A | HOH3247 |
| A | HOH3328 |
| B | HIS1388 |
| A | GLY158 |
| A | SER159 |
| A | SER209 |
| A | LYS210 |
| A | THR211 |
| A | THR214 |
| A | GLY271 |
| A | ARG272 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE S6P B 2001 |
| Chain | Residue |
| A | HIS388 |
| B | GLY1157 |
| B | GLY1158 |
| B | SER1159 |
| B | SER1209 |
| B | LYS1210 |
| B | THR1211 |
| B | THR1214 |
| B | GLY1271 |
| B | ARG1272 |
| B | GLN1353 |
| B | GLU1357 |
| B | HOH3126 |
| B | HOH3165 |
| B | HOH3182 |
| B | HOH3194 |
| B | HOH3244 |
| B | HOH3268 |
| B | HOH3305 |
Functional Information from PROSITE/UniProt
| site_id | PS00174 |
| Number of Residues | 18 |
| Details | P_GLUCOSE_ISOMERASE_2 Phosphoglucose isomerase signature 2. GvVWdinsFDQwGVElgK |
| 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":"11327814","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11425306","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"11327814","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11425306","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11425306","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HOX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P06745","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| 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_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P06744","evidenceCode":"ECO:0000250"}]} |
| 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":"UniProtKB","id":"P06745","evidenceCode":"ECO:0000250"}]} |
| 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 | GLY1271 | |
| B | LYS1518 | |
| B | LYS1210 | |
| B | GLU1216 | |
| B | GLU1357 | |
| B | ARG1272 |
| 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 | HIS1388 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 842 |
| Chain | Residue | Details |
| A | LYS210 | electrostatic stabiliser |
| A | GLU216 | modifies pKa |
| A | GLY271 | electrostatic stabiliser |
| A | ARG272 | electrostatic stabiliser |
| A | GLU357 | proton acceptor, proton donor |
| A | HIS388 | proton acceptor, proton donor |
| A | LYS518 | proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 842 |
| Chain | Residue | Details |
| B | LYS1210 | electrostatic stabiliser |
| B | GLU1216 | modifies pKa |
| B | GLY1271 | electrostatic stabiliser |
| B | ARG1272 | electrostatic stabiliser |
| B | GLU1357 | proton acceptor, proton donor |
| B | HIS1388 | proton acceptor, proton donor |
| B | LYS1518 | proton acceptor, proton donor |
