1TXG
Structure of glycerol-3-phosphate dehydrogenase from Archaeoglobus fulgidus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006072 | biological_process | glycerol-3-phosphate metabolic process |
| A | 0006650 | biological_process | glycerophospholipid metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0046167 | biological_process | glycerol-3-phosphate biosynthetic process |
| A | 0046168 | biological_process | glycerol-3-phosphate catabolic process |
| A | 0047952 | molecular_function | glycerol-3-phosphate dehydrogenase [NAD(P)+] activity |
| A | 0051287 | molecular_function | NAD binding |
| A | 0141153 | molecular_function | glycerol-3-phosphate dehydrogenase (NADP+) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006072 | biological_process | glycerol-3-phosphate metabolic process |
| B | 0006650 | biological_process | glycerophospholipid metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0046167 | biological_process | glycerol-3-phosphate biosynthetic process |
| B | 0046168 | biological_process | glycerol-3-phosphate catabolic process |
| B | 0047952 | molecular_function | glycerol-3-phosphate dehydrogenase [NAD(P)+] activity |
| B | 0051287 | molecular_function | NAD binding |
| B | 0141153 | molecular_function | glycerol-3-phosphate dehydrogenase (NADP+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1001 |
| Chain | Residue |
| B | ARG147 |
| B | HOH1175 |
| B | HOH1292 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1002 |
| Chain | Residue |
| A | LYS53 |
| A | ASN55 |
| A | HOH1070 |
| A | HOH1126 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1003 |
| Chain | Residue |
| A | ASN193 |
| A | HOH1078 |
| A | HOH1239 |
| A | LYS105 |
| A | LYS192 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1004 |
| Chain | Residue |
| A | ARG256 |
| A | GLY257 |
| A | GLY258 |
| A | HOH1052 |
| A | HOH1159 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1005 |
| Chain | Residue |
| A | ARG203 |
| A | ARG256 |
| A | GOL1009 |
| A | HOH1067 |
| A | HOH1158 |
| A | HOH1334 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1006 |
| Chain | Residue |
| B | ARG256 |
| B | GLY257 |
| B | GLY258 |
| B | HOH1065 |
| B | HOH1197 |
| B | HOH1201 |
| B | HOH1243 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1007 |
| Chain | Residue |
| B | LYS105 |
| B | LYS192 |
| B | ASN193 |
| B | HOH1120 |
| B | HOH1145 |
| B | HOH1280 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1008 |
| Chain | Residue |
| B | GLY258 |
| B | ARG259 |
| B | HOH1341 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NH4 B 1011 |
| Chain | Residue |
| B | LEU115 |
| B | THR116 |
| B | GLU119 |
| B | HOH1114 |
| B | HOH1381 |
| B | HOH1382 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1009 |
| Chain | Residue |
| A | ALA200 |
| A | ARG203 |
| A | LYS217 |
| A | PHE255 |
| A | SO41005 |
| A | HOH1020 |
| A | HOH1031 |
| A | HOH1112 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 1010 |
| Chain | Residue |
| B | ALA200 |
| B | ARG203 |
| B | LYS217 |
| B | PHE255 |
| B | HOH1022 |
| B | HOH1059 |
| B | HOH1248 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00394","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"A0A0F6AK91","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1evy |
| Chain | Residue | Details |
| A | LYS192 | |
| A | THR254 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1evy |
| Chain | Residue | Details |
| B | LYS192 | |
| B | THR254 |
