4DLB
Structure of S-nitrosoglutathione reductase from tomato (Solanum lycopersicum) crystallized in presence of NADH and glutathione
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004024 | molecular_function | alcohol dehydrogenase (NAD+) activity, zinc-dependent |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006069 | biological_process | obsolete ethanol oxidation |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016491 | molecular_function | oxidoreductase 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 |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004024 | molecular_function | alcohol dehydrogenase (NAD+) activity, zinc-dependent |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006069 | biological_process | obsolete ethanol oxidation |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046294 | biological_process | formaldehyde catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051903 | molecular_function | S-(hydroxymethyl)glutathione dehydrogenase (NAD(P)+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | CYS47 |
| A | HIS69 |
| A | CYS177 |
| A | HOH699 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 402 |
| Chain | Residue |
| A | CYS99 |
| A | CYS102 |
| A | CYS105 |
| A | CYS113 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD A 403 |
| Chain | Residue |
| A | THR49 |
| A | TYR95 |
| A | CYS177 |
| A | THR181 |
| A | GLY202 |
| A | GLY204 |
| A | THR205 |
| A | VAL206 |
| A | ASP226 |
| A | ILE227 |
| A | LYS231 |
| A | CYS271 |
| A | ILE272 |
| A | VAL277 |
| A | VAL295 |
| A | GLY296 |
| A | VAL297 |
| A | THR320 |
| A | ALA321 |
| A | PHE322 |
| A | ARG372 |
| A | HOH539 |
| A | HOH540 |
| A | HOH541 |
| A | HOH565 |
| A | HOH580 |
| A | HOH665 |
| A | HOH700 |
| A | HIS48 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 404 |
| Chain | Residue |
| A | ASP128 |
| A | LYS130 |
| A | LYS171 |
| A | ASP346 |
| A | ILE349 |
| A | ASN352 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 405 |
| Chain | Residue |
| A | TRP187 |
| A | LYS337 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 406 |
| Chain | Residue |
| A | GLU212 |
| A | LYS341 |
| A | GLU342 |
| A | LYS344 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 401 |
| Chain | Residue |
| B | CYS47 |
| B | HIS69 |
| B | GLU70 |
| B | CYS177 |
| B | HOH659 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 402 |
| Chain | Residue |
| B | CYS99 |
| B | CYS102 |
| B | CYS105 |
| B | CYS113 |
| site_id | AC9 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAD B 403 |
| Chain | Residue |
| B | HIS48 |
| B | THR49 |
| B | TYR95 |
| B | CYS177 |
| B | THR181 |
| B | GLY202 |
| B | GLY204 |
| B | THR205 |
| B | VAL206 |
| B | ASP226 |
| B | ILE227 |
| B | LYS231 |
| B | CYS271 |
| B | ILE272 |
| B | VAL277 |
| B | VAL295 |
| B | VAL297 |
| B | THR320 |
| B | ALA321 |
| B | PHE322 |
| B | ARG372 |
| B | HOH502 |
| B | HOH545 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 404 |
| Chain | Residue |
| B | THR120 |
| B | GLY121 |
| B | HIS142 |
| B | MET144 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 405 |
| Chain | Residue |
| B | ASP128 |
| B | LYS130 |
| B | LYS171 |
| B | ASP346 |
| B | ILE349 |
| B | ASN352 |
Functional Information from PROSITE/UniProt
| site_id | PS00059 |
| Number of Residues | 15 |
| Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEaAGIvesvGegV |
| Chain | Residue | Details |
| A | GLY68-VAL82 |
