5ZXL
Structure of GldA from E.coli
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005829 | cellular_component | cytosol |
A | 0006071 | biological_process | glycerol metabolic process |
A | 0008270 | molecular_function | zinc ion binding |
A | 0008888 | molecular_function | glycerol dehydrogenase (NAD+) activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0019147 | molecular_function | (R)-aminopropanol dehydrogenase activity |
A | 0019588 | biological_process | anaerobic glycerol catabolic process |
A | 0032991 | cellular_component | protein-containing complex |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0051289 | biological_process | protein homotetramerization |
A | 0051596 | biological_process | methylglyoxal catabolic process |
B | 0005829 | cellular_component | cytosol |
B | 0006071 | biological_process | glycerol metabolic process |
B | 0008270 | molecular_function | zinc ion binding |
B | 0008888 | molecular_function | glycerol dehydrogenase (NAD+) activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0019147 | molecular_function | (R)-aminopropanol dehydrogenase activity |
B | 0019588 | biological_process | anaerobic glycerol catabolic process |
B | 0032991 | cellular_component | protein-containing complex |
B | 0042802 | molecular_function | identical protein binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0051289 | biological_process | protein homotetramerization |
B | 0051596 | biological_process | methylglyoxal catabolic process |
C | 0005829 | cellular_component | cytosol |
C | 0006071 | biological_process | glycerol metabolic process |
C | 0008270 | molecular_function | zinc ion binding |
C | 0008888 | molecular_function | glycerol dehydrogenase (NAD+) activity |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
C | 0019147 | molecular_function | (R)-aminopropanol dehydrogenase activity |
C | 0019588 | biological_process | anaerobic glycerol catabolic process |
C | 0032991 | cellular_component | protein-containing complex |
C | 0042802 | molecular_function | identical protein binding |
C | 0046872 | molecular_function | metal ion binding |
C | 0051289 | biological_process | protein homotetramerization |
C | 0051596 | biological_process | methylglyoxal catabolic process |
D | 0005829 | cellular_component | cytosol |
D | 0006071 | biological_process | glycerol metabolic process |
D | 0008270 | molecular_function | zinc ion binding |
D | 0008888 | molecular_function | glycerol dehydrogenase (NAD+) activity |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
D | 0019147 | molecular_function | (R)-aminopropanol dehydrogenase activity |
D | 0019588 | biological_process | anaerobic glycerol catabolic process |
D | 0032991 | cellular_component | protein-containing complex |
D | 0042802 | molecular_function | identical protein binding |
D | 0046872 | molecular_function | metal ion binding |
D | 0051289 | biological_process | protein homotetramerization |
D | 0051596 | biological_process | methylglyoxal catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue ZN A 401 |
Chain | Residue |
A | ASP121 |
A | ASP171 |
A | HIS254 |
A | HIS271 |
A | GOL402 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue GOL A 402 |
Chain | Residue |
A | ASP121 |
A | PHE245 |
A | HIS254 |
A | ZN401 |
site_id | AC3 |
Number of Residues | 1 |
Details | binding site for residue GOL A 403 |
Chain | Residue |
A | ARG232 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue ZN B 401 |
Chain | Residue |
B | ASP121 |
B | ASP171 |
B | HIS254 |
B | HIS271 |
B | GOL402 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue GOL B 402 |
Chain | Residue |
B | ASP121 |
B | PHE245 |
B | HIS254 |
B | HIS271 |
B | ZN401 |
site_id | AC6 |
Number of Residues | 1 |
Details | binding site for residue GOL B 403 |
Chain | Residue |
B | ARG232 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue GOL B 404 |
Chain | Residue |
B | MET1 |
B | ARG3 |
D | GLY341 |
site_id | AC8 |
Number of Residues | 1 |
Details | binding site for residue SO4 B 405 |
Chain | Residue |
B | GLN311 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue ZN C 401 |
Chain | Residue |
C | ASP121 |
C | ASP171 |
C | HIS254 |
C | HIS271 |
C | GOL402 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue GOL C 402 |
Chain | Residue |
C | ASP121 |
C | PHE245 |
C | HIS254 |
C | HIS271 |
C | ZN401 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue GOL C 403 |
Chain | Residue |
C | ARG232 |
D | ARG3 |
D | GLN197 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue GOL C 404 |
Chain | Residue |
A | GLN347 |
C | MET1 |
C | ARG3 |
C | LYS194 |
D | GLU231 |
site_id | AD4 |
Number of Residues | 1 |
Details | binding site for residue GOL C 405 |
Chain | Residue |
C | ARG232 |
site_id | AD5 |
Number of Residues | 1 |
Details | binding site for residue SO4 C 406 |
Chain | Residue |
C | ARG184 |
site_id | AD6 |
Number of Residues | 1 |
Details | binding site for residue SO4 C 407 |
Chain | Residue |
C | GLN311 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue ZN D 401 |
Chain | Residue |
D | ASP171 |
D | HIS254 |
D | HIS271 |
D | GOL405 |
site_id | AD8 |
Number of Residues | 2 |
Details | binding site for residue ZN D 402 |
Chain | Residue |
D | HIS257 |
D | LYS274 |
site_id | AD9 |
Number of Residues | 1 |
Details | binding site for residue GOL D 403 |
Chain | Residue |
D | ARG232 |
site_id | AE1 |
Number of Residues | 1 |
Details | binding site for residue GOL D 404 |
Chain | Residue |
D | ARG31 |
site_id | AE2 |
Number of Residues | 6 |
Details | binding site for residue GOL D 405 |
Chain | Residue |
D | ASP121 |
D | ASP171 |
D | PHE245 |
D | HIS254 |
D | HIS271 |
D | ZN401 |
site_id | AE3 |
Number of Residues | 1 |
Details | binding site for residue CL D 406 |
Chain | Residue |
A | ASP54 |
site_id | AE4 |
Number of Residues | 1 |
Details | binding site for residue SO4 D 407 |
Chain | Residue |
D | GLN311 |
site_id | AE5 |
Number of Residues | 3 |
Details | binding site for residue SO4 D 408 |
Chain | Residue |
D | MET1 |
D | ARG3 |
D | LYS194 |
Functional Information from PROSITE/UniProt
site_id | PS00060 |
Number of Residues | 21 |
Details | ADH_IRON_2 Iron-containing alcohol dehydrogenases signature 2. SgVGfeSGgLAAahaVhNGlT |
Chain | Residue | Details |
A | SER241-THR261 |
site_id | PS00687 |
Number of Residues | 8 |
Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. FESGGLAA |
Chain | Residue | Details |
A | PHE245-ALA252 |
site_id | PS00913 |
Number of Residues | 29 |
Details | ADH_IRON_1 Iron-containing alcohol dehydrogenases signature 1. VIvDtkivagaParllAaGigDALatwfE |
Chain | Residue | Details |
A | VAL150-GLU178 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 32 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P32816 |
Chain | Residue | Details |
A | ASP37 | |
B | GLY94 | |
B | LYS95 | |
B | THR116 | |
B | SER119 | |
B | SER125 | |
B | LEU127 | |
B | TYR131 | |
C | ASP37 | |
C | GLY94 | |
C | LYS95 | |
A | GLY94 | |
C | THR116 | |
C | SER119 | |
C | SER125 | |
C | LEU127 | |
C | TYR131 | |
D | ASP37 | |
D | GLY94 | |
D | LYS95 | |
D | THR116 | |
D | SER119 | |
A | LYS95 | |
D | SER125 | |
D | LEU127 | |
D | TYR131 | |
A | THR116 | |
A | SER119 | |
A | SER125 | |
A | LEU127 | |
A | TYR131 | |
B | ASP37 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:30839292, ECO:0007744|PDB:5ZXL |
Chain | Residue | Details |
A | ASP121 | |
C | ASP171 | |
C | HIS254 | |
C | HIS271 | |
D | ASP121 | |
D | ASP171 | |
D | HIS254 | |
D | HIS271 | |
A | ASP171 | |
A | HIS254 | |
A | HIS271 | |
B | ASP121 | |
B | ASP171 | |
B | HIS254 | |
B | HIS271 | |
C | ASP121 |