1DPG
GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004345 | molecular_function | glucose-6-phosphate dehydrogenase activity |
A | 0005829 | cellular_component | cytosol |
A | 0006006 | biological_process | glucose metabolic process |
A | 0006098 | biological_process | pentose-phosphate shunt |
A | 0009051 | biological_process | pentose-phosphate shunt, oxidative branch |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
A | 0050661 | molecular_function | NADP binding |
B | 0004345 | molecular_function | glucose-6-phosphate dehydrogenase activity |
B | 0005829 | cellular_component | cytosol |
B | 0006006 | biological_process | glucose metabolic process |
B | 0006098 | biological_process | pentose-phosphate shunt |
B | 0009051 | biological_process | pentose-phosphate shunt, oxidative branch |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
B | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 A 2000 |
Chain | Residue |
A | GLU147 |
A | LYS148 |
A | ILE176 |
A | ASP177 |
A | HIS178 |
A | HIS240 |
A | TYR415 |
A | HOH2079 |
A | HOH2265 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 2002 |
Chain | Residue |
A | HIS178 |
A | TYR179 |
A | LYS182 |
A | LYS343 |
A | HOH2291 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 B 2001 |
Chain | Residue |
B | GLU147 |
B | LYS148 |
B | ILE176 |
B | ASP177 |
B | HIS178 |
B | HIS240 |
B | TYR415 |
B | HOH2172 |
B | HOH2216 |
Functional Information from PROSITE/UniProt
site_id | PS00069 |
Number of Residues | 7 |
Details | G6P_DEHYDROGENASE Glucose-6-phosphate dehydrogenase active site. DHYLGKE |
Chain | Residue | Details |
A | ASP177-GLU183 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:9485426 |
Chain | Residue | Details |
A | THR241 | |
B | THR241 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:11106478, ECO:0000269|PubMed:11320304, ECO:0000269|PubMed:9485426 |
Chain | Residue | Details |
A | GLY13 | |
A | GLN47 | |
A | VAL86 | |
B | GLY13 | |
B | GLN47 | |
B | VAL86 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:11320304 |
Chain | Residue | Details |
A | PRO149 | |
B | PRO149 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000305|PubMed:11106478 |
Chain | Residue | Details |
A | TYR179 | |
B | MET236 | |
B | ARG339 | |
B | GLN344 | |
A | GLU183 | |
A | VAL217 | |
A | MET236 | |
A | ARG339 | |
A | GLN344 | |
B | TYR179 | |
B | GLU183 | |
B | VAL217 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | a catalytic site defined by CSA, PubMed 7881907 |
Chain | Residue | Details |
A | ASP177 | |
A | HIS240 |
site_id | CSA2 |
Number of Residues | 2 |
Details | a catalytic site defined by CSA, PubMed 7881907 |
Chain | Residue | Details |
B | ASP177 | |
B | HIS240 |
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 843 |
Chain | Residue | Details |
A | ASP177 | modifies pKa |
A | HIS178 | transition state stabiliser |
A | HIS240 | proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 843 |
Chain | Residue | Details |
B | ASP177 | modifies pKa |
B | HIS178 | transition state stabiliser |
B | HIS240 | proton acceptor, proton donor |