8CON
Crystal structure of alcohol dehydrogenase from Arabidopsis thaliana in complex with NADH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0001666 | biological_process | response to hypoxia |
| A | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006970 | biological_process | response to osmotic stress |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009409 | biological_process | response to cold |
| A | 0009413 | biological_process | response to flooding |
| A | 0009414 | biological_process | response to water deprivation |
| A | 0009651 | biological_process | response to salt stress |
| A | 0009737 | biological_process | response to abscisic acid |
| A | 0009744 | biological_process | response to sucrose |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0031000 | biological_process | response to caffeine |
| A | 0032355 | biological_process | response to estradiol |
| A | 0042542 | biological_process | response to hydrogen peroxide |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071456 | biological_process | cellular response to hypoxia |
| A | 1900039 | biological_process | positive regulation of cellular response to hypoxia |
Functional Information from PROSITE/UniProt
| site_id | PS00059 |
| Number of Residues | 15 |
| Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEaGGIvesvGegV |
| Chain | Residue | Details |
| A | GLY68-VAL82 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25447145, ECO:0007744|PDB:4RQT, ECO:0007744|PDB:4RQU |
| Chain | Residue | Details |
| A | CYS47 | |
| A | HIS69 | |
| A | CYS99 | |
| A | CYS102 | |
| A | CYS105 | |
| A | CYS113 | |
| A | CYS177 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25447145, ECO:0007744|PDB:4RQU |
| Chain | Residue | Details |
| A | THR49 | |
| A | GLY202 | |
| A | ASP226 | |
| A | ARG231 | |
| A | THR272 | |
| A | VAL295 | |
| A | PHE322 | |
| A | ARG372 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylserine => ECO:0007744|PubMed:22223895 |
| Chain | Residue | Details |
| A | SER2 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18433157, ECO:0007744|PubMed:19245862 |
| Chain | Residue | Details |
| A | SER229 |
