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 | 0006094 | biological_process | gluconeogenesis |
A | 0006127 | biological_process | glycerol-3-phosphate shuttle |
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 | 0047952 | molecular_function | glycerol-3-phosphate dehydrogenase [NAD(P)+] activity |
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 |
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 | 0006094 | biological_process | gluconeogenesis |
B | 0006127 | biological_process | glycerol-3-phosphate shuttle |
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 | 0045821 | biological_process | positive regulation of glycolytic 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 | 0070062 | cellular_component | extracellular exosome |
B | 0071320 | biological_process | cellular response to cAMP |
B | 0071356 | biological_process | cellular response to tumor necrosis factor |
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 | ACT_SITE: Proton acceptor => ECO:0000305 |
Chain | Residue | Details |
A | LYS204 | |
B | LYS204 |
site_id | SWS_FT_FI2 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16460752 |
Chain | Residue | Details |
A | GLY10 | |
B | PHE97 | |
B | ALA153 | |
B | ARG269 | |
B | LYS296 | |
B | GLN298 | |
A | PHE41 | |
A | PHE97 | |
A | ALA153 | |
A | ARG269 | |
A | LYS296 | |
A | GLN298 | |
B | GLY10 | |
B | PHE41 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS120 | |
B | LYS120 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER154 | |
B | SER154 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P13707 |
Chain | Residue | Details |
A | LYS289 | |
B | LYS289 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:O35077 |
Chain | Residue | Details |
A | TYR326 | |
B | TYR326 |