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 | 0046294 | biological_process | formaldehyde catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051903 | molecular_function | S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity |
| A | 0071456 | biological_process | cellular response to hypoxia |
| A | 0120542 | molecular_function | ethanol dehydrogenase (NAD+) activity |
| 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 site: {"evidences":[{"source":"PubMed","id":"25447145","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38308388","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4RQT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RQU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8CON","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25447145","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4RQU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25447145","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38308388","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4RQU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8CON","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"38308388","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8CON","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18433157","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19245862","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
