1Z82
Crystal structure of glycerol-3-phosphate dehydrogenase (TM0378) from THERMOTOGA MARITIMA at 2.00 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0008654 | biological_process | phospholipid biosynthetic 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 | 0000166 | molecular_function | nucleotide binding |
| 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 | 0008654 | biological_process | phospholipid biosynthetic 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 | 32 |
| Details | BINDING SITE FOR RESIDUE NDP A 500 |
| Chain | Residue |
| A | ALA10 |
| A | TYR80 |
| A | HIS84 |
| A | SER99 |
| A | LYS100 |
| A | SER129 |
| A | HIS130 |
| A | ALA131 |
| A | ARG243 |
| A | ASN265 |
| A | GLN266 |
| A | GLY11 |
| A | VAL267 |
| A | GLU269 |
| A | HOH621 |
| A | HOH626 |
| A | HOH629 |
| A | HOH634 |
| A | HOH641 |
| A | HOH648 |
| A | HOH651 |
| A | HOH663 |
| A | SER12 |
| A | HOH664 |
| A | HOH687 |
| B | G3P600 |
| A | TRP13 |
| A | ARG33 |
| A | ARG34 |
| A | TYR49 |
| A | ALA75 |
| A | PRO77 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE G3H A 600 |
| Chain | Residue |
| A | HOH613 |
| B | LYS100 |
| B | GLY127 |
| B | PRO128 |
| B | SER129 |
| B | HIS130 |
| B | LYS179 |
| B | ASN180 |
| B | ASP232 |
| B | THR236 |
| B | TYR241 |
| B | SER242 |
| B | ARG243 |
| B | ASN244 |
| B | NDP500 |
| B | HOH618 |
| B | HOH635 |
| site_id | AC3 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NDP B 500 |
| Chain | Residue |
| A | ARG87 |
| A | G3H600 |
| B | ALA10 |
| B | GLY11 |
| B | SER12 |
| B | TRP13 |
| B | ARG33 |
| B | ARG34 |
| B | TYR49 |
| B | ALA75 |
| B | PRO77 |
| B | TYR80 |
| B | GLU83 |
| B | HIS84 |
| B | SER99 |
| B | LYS100 |
| B | SER129 |
| B | HIS130 |
| B | ALA131 |
| B | ARG243 |
| B | ASN265 |
| B | GLN266 |
| B | VAL267 |
| B | GLU269 |
| B | HOH618 |
| B | HOH620 |
| B | HOH621 |
| B | HOH633 |
| B | HOH635 |
| B | HOH636 |
| B | HOH638 |
| B | HOH652 |
| B | HOH653 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE G3P B 600 |
| Chain | Residue |
| A | LYS100 |
| A | GLY127 |
| A | SER129 |
| A | HIS130 |
| A | LYS179 |
| A | ASP232 |
| A | THR236 |
| A | TYR241 |
| A | SER242 |
| A | ARG243 |
| A | ASN244 |
| A | NDP500 |
| A | HOH621 |
| A | HOH626 |
| B | HOH630 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MRD B 601 |
| Chain | Residue |
| B | GLU293 |
| B | SER307 |
| B | MSE308 |
| B | LEU311 |
| B | MRD602 |
| B | HOH684 |
| B | ALA185 |
| B | ILE188 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MRD A 601 |
| Chain | Residue |
| A | ALA185 |
| A | ILE188 |
| A | LEU189 |
| A | GLU293 |
| A | VAL294 |
| A | SER307 |
| A | MSE308 |
| A | LEU311 |
| A | HOH735 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MRD B 602 |
| Chain | Residue |
| A | THR140 |
| B | MSE312 |
| B | MRD601 |
| B | HOH684 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MRD B 603 |
| Chain | Residue |
| B | ARG243 |
| B | ARG246 |
| B | LEU260 |
| B | SER263 |
| B | SER264 |
| B | GLN266 |
| B | VAL268 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MRD B 604 |
| Chain | Residue |
| A | VAL43 |
| A | SER44 |
| B | MSE3 |
| B | GLU151 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD A 602 |
| Chain | Residue |
| A | ARG205 |
| A | LEU311 |
| A | HOH735 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD A 603 |
| Chain | Residue |
| A | ARG243 |
| A | ARG246 |
| A | LEU260 |
| A | SER263 |
| A | SER264 |
| A | GLN266 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MPD A 604 |
| Chain | Residue |
| A | GLY254 |
| A | PHE255 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00394 |
| Chain | Residue | Details |
| A | LYS179 | |
| B | LYS179 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 30 |
| Details | BINDING: BINDING => ECO:0000269|Ref.2, ECO:0007744|PDB:1Z82 |
| Chain | Residue | Details |
| A | SER12 | |
| A | ASP232 | |
| A | SER242 | |
| A | ARG243 | |
| A | ASN244 | |
| A | VAL267 | |
| A | GLU269 | |
| B | SER12 | |
| B | TRP13 | |
| B | ARG33 | |
| B | ARG34 | |
| A | TRP13 | |
| B | TYR49 | |
| B | LYS100 | |
| B | GLY127 | |
| B | SER129 | |
| B | ALA131 | |
| B | ASP232 | |
| B | SER242 | |
| B | ARG243 | |
| B | ASN244 | |
| B | VAL267 | |
| A | ARG33 | |
| B | GLU269 | |
| A | ARG34 | |
| A | TYR49 | |
| A | LYS100 | |
| A | GLY127 | |
| A | SER129 | |
| A | ALA131 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0007744|PDB:1Z82 |
| Chain | Residue | Details |
| A | LYS179 | |
| B | LYS179 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1evy |
| Chain | Residue | Details |
| A | LYS179 | |
| A | THR236 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1evy |
| Chain | Residue | Details |
| B | LYS179 | |
| B | THR236 |
