2Q8N
Crystal structure of Glucose-6-phosphate isomerase (EC 5.3.1.9) (TM1385) from Thermotoga maritima at 1.82 A resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004347 | molecular_function | glucose-6-phosphate isomerase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006094 | biological_process | gluconeogenesis |
A | 0006096 | biological_process | glycolytic process |
A | 0016853 | molecular_function | isomerase 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 | 0004347 | molecular_function | glucose-6-phosphate isomerase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006094 | biological_process | gluconeogenesis |
B | 0006096 | biological_process | glycolytic process |
B | 0016853 | molecular_function | isomerase 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 |
C | 0004347 | molecular_function | glucose-6-phosphate isomerase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006094 | biological_process | gluconeogenesis |
C | 0006096 | biological_process | glycolytic process |
C | 0016853 | molecular_function | isomerase activity |
C | 0048029 | molecular_function | monosaccharide binding |
C | 0051156 | biological_process | glucose 6-phosphate metabolic process |
C | 0097367 | molecular_function | carbohydrate derivative binding |
C | 1901135 | biological_process | carbohydrate derivative metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 449 |
Chain | Residue |
B | ARG187 |
B | HOH557 |
C | ARG50 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C 449 |
Chain | Residue |
C | SER138 |
C | THR141 |
C | LYS422 |
C | HOH550 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 449 |
Chain | Residue |
A | LYS422 |
A | HOH522 |
A | HOH543 |
A | SER138 |
A | THR141 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 450 |
Chain | Residue |
B | SER138 |
B | THR141 |
B | LYS422 |
B | HOH535 |
B | HOH598 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 450 |
Chain | Residue |
A | THR97 |
A | ARG98 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 450 |
Chain | Residue |
C | THR97 |
C | ARG98 |
C | HOH530 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 451 |
Chain | Residue |
A | LYS302 |
A | HOH533 |
B | LYS302 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL C 451 |
Chain | Residue |
C | LYS302 |
C | HOH536 |
site_id | AC9 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE 2PE C 452 |
Chain | Residue |
C | LEU82 |
C | LEU82 |
C | HIS85 |
C | HIS85 |
C | TYR86 |
C | LEU91 |
C | LEU91 |
C | GLU95 |
C | VAL107 |
C | VAL107 |
C | PHE108 |
C | PHE108 |
C | VAL109 |
C | VAL109 |
C | SER120 |
C | SER120 |
C | VAL121 |
site_id | BC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE 2PE B 452 |
Chain | Residue |
A | LEU91 |
A | GLU95 |
A | VAL107 |
A | PHE108 |
A | VAL109 |
A | SER120 |
B | HIS85 |
B | LEU91 |
B | GLU95 |
B | VAL107 |
B | PHE108 |
B | VAL109 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE 2PE A 453 |
Chain | Residue |
A | ASN321 |
B | PHE295 |
Functional Information from PROSITE/UniProt
site_id | PS00174 |
Number of Residues | 18 |
Details | P_GLUCOSE_ISOMERASE_2 Phosphoglucose isomerase signature 2. GyLLeinpFDQpGVElgK |
Chain | Residue | Details |
A | GLY405-LYS422 |
site_id | PS00230 |
Number of Residues | 10 |
Details | MAP1B_NEURAXIN Neuraxin and MAP1B proteins repeated region signature. GYtYEIKERS |
Chain | Residue | Details |
A | GLY433-SER442 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00473, ECO:0000305|PubMed:33422670 |
Chain | Residue | Details |
A | GLU281 | |
B | GLU281 | |
C | GLU281 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00473, ECO:0000305|PubMed:33422670 |
Chain | Residue | Details |
A | HIS310 | |
A | LYS422 | |
B | HIS310 | |
B | LYS422 | |
C | HIS310 | |
C | LYS422 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1dqr |
Chain | Residue | Details |
C | LYS422 | |
C | GLU281 | |
C | ARG198 | |
C | GLU143 | |
C | GLY197 | |
C | LYS137 |
site_id | CSA2 |
Number of Residues | 7 |
Details | Annotated By Reference To The Literature 1dqr |
Chain | Residue | Details |
A | HIS310 | |
B | GLU281 | |
B | LYS422 | |
B | GLU143 | |
B | ARG198 | |
B | GLY197 | |
B | LYS137 |
site_id | CSA3 |
Number of Residues | 7 |
Details | Annotated By Reference To The Literature 1dqr |
Chain | Residue | Details |
A | LYS422 | |
A | GLU281 | |
A | ARG198 | |
A | GLU143 | |
A | GLY197 | |
A | LYS137 | |
B | HIS310 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1dqr |
Chain | Residue | Details |
C | HIS310 |