4DL9
Crystal structure of S-nitrosoglutathione reductase from tomato (Solanum lycopersicum) in complex with NAD+
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 | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | CYS47 |
| A | HIS69 |
| A | GLU70 |
| A | CYS177 |
| A | ARG372 |
| 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 | 34 |
| Details | BINDING SITE FOR RESIDUE NAD A 403 |
| Chain | Residue |
| 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 | GLY273 |
| A | VAL277 |
| A | VAL295 |
| A | GLY296 |
| A | VAL297 |
| A | THR320 |
| A | ALA321 |
| A | PHE322 |
| A | ARG372 |
| A | HOH501 |
| A | HOH504 |
| A | HOH505 |
| A | HOH506 |
| A | HOH510 |
| A | HOH511 |
| A | HOH512 |
| A | HOH562 |
| A | HOH666 |
| A | HOH685 |
| A | HOH692 |
| A | HOH778 |
| A | HOH793 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 404 |
| Chain | Residue |
| A | TRP187 |
| A | ALA216 |
| A | ALA217 |
| A | LYS337 |
| A | HOH582 |
| A | HOH708 |
| A | HOH736 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MES A 405 |
| Chain | Residue |
| A | ARG307 |
| A | PHE309 |
| A | HOH646 |
| B | GLU60 |
| B | SER300 |
| B | GLY301 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 401 |
| Chain | Residue |
| B | CYS47 |
| B | HIS69 |
| B | GLU70 |
| B | CYS177 |
| B | ARG372 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 402 |
| Chain | Residue |
| B | CYS99 |
| B | CYS102 |
| B | CYS105 |
| B | CYS113 |
| site_id | AC8 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD B 403 |
| Chain | Residue |
| 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 | GLY296 |
| B | VAL297 |
| B | THR320 |
| B | ALA321 |
| B | PHE322 |
| B | ARG372 |
| B | HOH504 |
| B | HOH505 |
| B | HOH508 |
| B | HOH509 |
| B | HOH638 |
| B | HOH653 |
| B | HOH689 |
| B | HOH712 |
| B | HOH713 |
| B | HOH725 |
| B | HOH756 |
| B | HOH809 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 404 |
| Chain | Residue |
| B | LYS337 |
| B | HOH555 |
| B | TRP187 |
| B | ALA217 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MES B 405 |
| Chain | Residue |
| A | GLU60 |
| A | SER300 |
| A | GLY301 |
| B | ARG307 |
| B | PHE309 |
| B | HOH686 |
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 |
