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 | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0044281 | biological_process | small molecule metabolic process |
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 | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0044281 | biological_process | small molecule metabolic process |
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 |