8GV3
The cryo-EM structure of GSNOR with NYY001
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| A | 0005504 | molecular_function | fatty acid binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0010430 | biological_process | fatty acid omega-oxidation |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0018467 | molecular_function | formaldehyde dehydrogenase (NAD+) activity |
| A | 0044281 | biological_process | small molecule metabolic process |
| A | 0046294 | biological_process | formaldehyde catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051775 | biological_process | response to redox state |
| A | 0051903 | molecular_function | S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0080007 | molecular_function | S-nitrosoglutathione reductase (NADH) activity |
| A | 0106321 | molecular_function | S-(hydroxymethyl)glutathione dehydrogenase (NADP+) activity |
| A | 0106322 | molecular_function | S-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity |
| B | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| B | 0005504 | molecular_function | fatty acid binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0010430 | biological_process | fatty acid omega-oxidation |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0018467 | molecular_function | formaldehyde dehydrogenase (NAD+) activity |
| B | 0044281 | biological_process | small molecule metabolic process |
| B | 0046294 | biological_process | formaldehyde catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051775 | biological_process | response to redox state |
| B | 0051903 | molecular_function | S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0080007 | molecular_function | S-nitrosoglutathione reductase (NADH) activity |
| B | 0106321 | molecular_function | S-(hydroxymethyl)glutathione dehydrogenase (NADP+) activity |
| B | 0106322 | molecular_function | S-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity |
Functional Information from PROSITE/UniProt
| site_id | PS00059 |
| Number of Residues | 15 |
| Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEgAGIvesvGegV |
| Chain | Residue | Details |
| A | GLY65-VAL79 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"3365377","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for FDH activity and activation by fatty acids","evidences":[{"source":"PubMed","id":"8460164","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8494891","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P28474","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 12 |
| Details | M-CSA 464 |
| Chain | Residue | Details |
| A | CYS44 | metal ligand |
| A | ARG114 | activator |
| A | CYS173 | metal ligand |
| A | ARG368 | steric role |
| A | HIS45 | proton shuttle (general acid/base) |
| A | THR46 | proton shuttle (general acid/base) |
| A | HIS66 | metal ligand |
| A | GLU67 | metal ligand |
| A | CYS96 | metal ligand |
| A | CYS99 | metal ligand |
| A | CYS102 | metal ligand |
| A | CYS110 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 12 |
| Details | M-CSA 464 |
| Chain | Residue | Details |
| B | CYS44 | metal ligand |
| B | ARG114 | activator |
| B | CYS173 | metal ligand |
| B | ARG368 | steric role |
| B | HIS45 | proton shuttle (general acid/base) |
| B | THR46 | proton shuttle (general acid/base) |
| B | HIS66 | metal ligand |
| B | GLU67 | metal ligand |
| B | CYS96 | metal ligand |
| B | CYS99 | metal ligand |
| B | CYS102 | metal ligand |
| B | CYS110 | metal ligand |
