4L0Q
Crystal structure of S-nitrosoglutathione reductase from Arabidopsis thaliana, C370A/C373A double mutant
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
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 |
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 | 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 |
B | 0106321 | molecular_function | S-(hydroxymethyl)glutathione dehydrogenase (NADP+) activity |
B | 0106322 | molecular_function | S-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 401 |
Chain | Residue |
A | CYS99 |
A | CYS102 |
A | CYS105 |
A | CYS113 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 402 |
Chain | Residue |
A | CYS47 |
A | HIS69 |
A | GLU70 |
A | CYS177 |
site_id | AC3 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE NAD A 403 |
Chain | Residue |
A | TYR95 |
A | CYS177 |
A | THR181 |
A | GLY202 |
A | LEU203 |
A | GLY204 |
A | THR205 |
A | VAL206 |
A | ASP226 |
A | ILE227 |
A | LYS231 |
A | CYS271 |
A | ILE272 |
A | VAL277 |
A | VAL295 |
A | VAL297 |
A | THR320 |
A | ALA321 |
A | PHE322 |
A | ARG372 |
A | HOH507 |
A | HOH563 |
A | HOH575 |
A | HOH594 |
A | HOH600 |
A | HOH609 |
A | HOH611 |
A | HOH620 |
A | HOH671 |
A | HIS48 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 404 |
Chain | Residue |
A | LYS318 |
A | HOH582 |
A | HOH637 |
B | VAL316 |
B | LYS318 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 A 405 |
Chain | Residue |
A | SER276 |
A | ARG279 |
A | SER305 |
A | HOH501 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 A 406 |
Chain | Residue |
A | HIS249 |
A | ASP250 |
A | LYS251 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 401 |
Chain | Residue |
B | CYS99 |
B | CYS102 |
B | CYS105 |
B | CYS113 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 402 |
Chain | Residue |
B | CYS47 |
B | HIS69 |
B | GLU70 |
B | CYS177 |
site_id | AC9 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAD B 403 |
Chain | Residue |
B | HIS48 |
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 | HOH514 |
B | HOH532 |
B | HOH535 |
B | HOH556 |
B | HOH561 |
B | HOH574 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 B 404 |
Chain | Residue |
B | SER276 |
B | ARG279 |
B | HOH525 |
B | HOH690 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 B 405 |
Chain | Residue |
B | HIS249 |
B | ASP250 |
B | LYS251 |
site_id | BC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 B 406 |
Chain | Residue |
B | HOH517 |
B | HOH627 |
A | ARG307 |
A | PRO308 |
A | PHE309 |
B | ALA298 |
B | ALA299 |
B | SER300 |
B | GLY301 |
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 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000269|Ref.13, ECO:0007744|PDB:3UKO, ECO:0007744|PDB:4GL4, ECO:0007744|PDB:4JJI, ECO:0007744|PDB:4L0Q |
Chain | Residue | Details |
A | CYS47 | |
A | GLY202 | |
A | ASP226 | |
A | ILE272 | |
A | VAL295 | |
A | THR320 | |
B | CYS47 | |
B | HIS48 | |
B | HIS69 | |
B | GLU70 | |
B | CYS99 | |
A | HIS48 | |
B | CYS102 | |
B | CYS105 | |
B | CYS113 | |
B | CYS177 | |
B | GLY202 | |
B | ASP226 | |
B | ILE272 | |
B | VAL295 | |
B | THR320 | |
A | HIS69 | |
A | GLU70 | |
A | CYS99 | |
A | CYS102 | |
A | CYS105 | |
A | CYS113 | |
A | CYS177 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P06525 |
Chain | Residue | Details |
A | THR49 | |
B | THR49 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|Ref.13, ECO:0007744|PDB:3UKO, ECO:0007744|PDB:4JJI, ECO:0007744|PDB:4L0Q |
Chain | Residue | Details |
A | LYS231 | |
A | ARG372 | |
B | LYS231 | |
B | ARG372 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:22223895 |
Chain | Residue | Details |
A | ALA2 | |
B | ALA2 |