1X0X
Co-Structure of Homo Sapiens Glycerol-3-Phosphate Dehydrogenase 1 complex with NAD
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004368 | molecular_function | glycerol-3-phosphate dehydrogenase (quinone) activity |
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 | 0006094 | biological_process | gluconeogenesis |
A | 0006116 | biological_process | NADH oxidation |
A | 0006127 | biological_process | glycerophosphate shuttle |
A | 0006734 | biological_process | NADH 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 | 0045821 | biological_process | positive regulation of glycolytic process |
A | 0046168 | biological_process | glycerol-3-phosphate catabolic process |
A | 0046486 | biological_process | glycerolipid metabolic process |
A | 0051287 | molecular_function | NAD binding |
A | 0070062 | cellular_component | extracellular exosome |
A | 0071320 | biological_process | cellular response to cAMP |
A | 0071356 | biological_process | cellular response to tumor necrosis factor |
A | 0141152 | molecular_function | glycerol-3-phosphate dehydrogenase (NAD+) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 1001 |
Chain | Residue |
A | LYS20 |
A | HIS67 |
A | LYS68 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE SO4 A 1002 |
Chain | Residue |
A | HOH2010 |
A | HOH2022 |
A | HOH2039 |
A | HOH2049 |
A | HOH2076 |
A | HOH2134 |
A | LYS204 |
A | ASN205 |
A | THR264 |
A | GLY268 |
A | ARG269 |
A | ASN270 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 1003 |
Chain | Residue |
A | LYS240 |
A | VAL247 |
A | SER248 |
A | SER249 |
A | HOH2175 |
A | HOH2179 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 1004 |
Chain | Residue |
A | ARG271 |
A | LYS272 |
A | HOH2017 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 1005 |
Chain | Residue |
A | ASN13 |
A | GLN295 |
A | HOH2065 |
A | HOH2096 |
A | HOH2211 |
site_id | AC6 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE NAD A 2001 |
Chain | Residue |
A | SER11 |
A | GLY12 |
A | ASN13 |
A | TRP14 |
A | GLY15 |
A | PHE41 |
A | TYR63 |
A | VAL93 |
A | PRO94 |
A | PHE97 |
A | ILE119 |
A | LYS120 |
A | ASN151 |
A | ALA153 |
A | ARG269 |
A | GLY294 |
A | GLN295 |
A | LYS296 |
A | GLN298 |
A | HOH2007 |
A | HOH2011 |
A | HOH2012 |
A | HOH2022 |
A | HOH2023 |
A | HOH2039 |
A | HOH2044 |
A | HOH2087 |
A | HOH2134 |
A | HOH2135 |
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 | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000305 |
Chain | Residue | Details |
A | LYS204 |
site_id | SWS_FT_FI2 |
Number of Residues | 7 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16460752 |
Chain | Residue | Details |
A | GLY10 | |
A | PHE41 | |
A | PHE97 | |
A | ALA153 | |
A | ARG269 | |
A | LYS296 | |
A | GLN298 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS120 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER154 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P13707 |
Chain | Residue | Details |
A | LYS289 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:O35077 |
Chain | Residue | Details |
A | TYR326 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1evy |
Chain | Residue | Details |
A | LYS204 | |
A | THR264 |