6E8Z
Binary complex of Human glycerol 3-phosphate dehydrogenase with NAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein 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 | 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 | 0042803 | molecular_function | protein homodimerization activity |
| 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 | 0070062 | cellular_component | extracellular exosome |
| A | 0141152 | molecular_function | glycerol-3-phosphate dehydrogenase (NAD+) activity |
| B | 0005515 | molecular_function | protein 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 | 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 | 0042803 | molecular_function | protein homodimerization activity |
| 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 | 0070062 | cellular_component | extracellular exosome |
| B | 0141152 | molecular_function | glycerol-3-phosphate dehydrogenase (NAD+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue NAD A 401 |
| Chain | Residue |
| A | SER11 |
| A | ILE119 |
| A | LYS120 |
| A | ASN151 |
| A | ILE152 |
| A | ALA153 |
| A | HOH505 |
| A | HOH527 |
| A | HOH538 |
| A | HOH547 |
| A | HOH553 |
| A | GLY12 |
| A | HOH554 |
| A | ASN13 |
| A | TRP14 |
| A | TRP39 |
| A | PHE41 |
| A | VAL93 |
| A | PRO94 |
| A | PHE97 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 A 402 |
| Chain | Residue |
| A | LEU131 |
| A | GLU134 |
| A | ASP195 |
| A | PHE242 |
| A | SER244 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | ALA237 |
| A | LYS318 |
| A | PRO346 |
| A | GLU347 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | LYS240 |
| A | PRO246 |
| A | VAL247 |
| A | HOH511 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | LYS120 |
| A | GLY149 |
| A | ASN151 |
| A | LYS204 |
| A | ASP260 |
| A | THR263 |
| A | THR264 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue K A 406 |
| Chain | Residue |
| A | ALA26 |
| A | ALA27 |
| A | LEU29 |
| A | PHE32 |
| A | PRO34 |
| A | ASN344 |
| site_id | AC7 |
| Number of Residues | 21 |
| Details | binding site for residue NAD B 401 |
| Chain | Residue |
| B | SER11 |
| B | GLY12 |
| B | ASN13 |
| B | TRP14 |
| B | TRP39 |
| B | PHE41 |
| B | TYR63 |
| B | VAL93 |
| B | PRO94 |
| B | PHE97 |
| B | ILE119 |
| B | LYS120 |
| B | ASN151 |
| B | ILE152 |
| B | ALA153 |
| B | HOH505 |
| B | HOH511 |
| B | HOH517 |
| B | HOH533 |
| B | HOH545 |
| B | HOH586 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 B 402 |
| Chain | Residue |
| B | GLU134 |
| B | ASP195 |
| B | PHE242 |
| B | SER244 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| B | LYS318 |
| B | HIS345 |
| B | PRO346 |
| B | GLU347 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue K B 404 |
| Chain | Residue |
| B | ALA26 |
| B | ALA27 |
| B | LEU29 |
| B | PHE32 |
| B | HOH507 |
| B | HOH584 |
Functional Information from PROSITE/UniProt
| site_id | PS00957 |
| Number of Residues | 22 |
| Details | NAD_G3PDH NAD-dependent glycerol-3-phosphate dehydrogenase signature. GALKNVVAvGaGFcdGLgFGdN |
| Chain | Residue | Details |
| A | GLY201-ASN222 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16460752","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P13707","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"O35077","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






