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 | 0005737 | cellular_component | cytoplasm |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005829 | cellular_component | cytosol |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009536 | cellular_component | plastid |
| A | 0010286 | biological_process | heat acclimation |
| A | 0012501 | biological_process | programmed cell death |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0044281 | biological_process | small molecule metabolic process |
| A | 0046292 | biological_process | formaldehyde metabolic process |
| A | 0046294 | biological_process | formaldehyde catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048316 | biological_process | seed development |
| A | 0051903 | molecular_function | S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity |
| 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 | 0005737 | cellular_component | cytoplasm |
| B | 0005777 | cellular_component | peroxisome |
| B | 0005829 | cellular_component | cytosol |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009536 | cellular_component | plastid |
| B | 0010286 | biological_process | heat acclimation |
| B | 0012501 | biological_process | programmed cell death |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0044281 | biological_process | small molecule metabolic process |
| B | 0046292 | biological_process | formaldehyde metabolic process |
| B | 0046294 | biological_process | formaldehyde catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048316 | biological_process | seed development |
| B | 0051903 | molecular_function | S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity |
| 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 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 | 14 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:38308388, ECO:0000269|Ref.13, ECO:0007744|PDB:3UKO, ECO:0007744|PDB:4GL4, ECO:0007744|PDB:4JJI, ECO:0007744|PDB:4L0Q, ECO:0007744|PDB:8CO4 |
| Chain | Residue | Details |
| A | CYS47 | |
| B | CYS99 | |
| B | CYS102 | |
| B | CYS105 | |
| B | CYS113 | |
| B | CYS177 | |
| A | HIS69 | |
| A | CYS99 | |
| A | CYS102 | |
| A | CYS105 | |
| A | CYS113 | |
| A | CYS177 | |
| B | CYS47 | |
| B | HIS69 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| 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 | HIS48 | |
| B | GLY202 | |
| B | ASP226 | |
| B | ILE272 | |
| B | VAL295 | |
| B | THR320 | |
| A | GLU70 | |
| A | GLY202 | |
| A | ASP226 | |
| A | ILE272 | |
| A | VAL295 | |
| A | THR320 | |
| B | HIS48 | |
| B | GLU70 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P06525 |
| Chain | Residue | Details |
| A | THR49 | |
| B | THR49 |
| site_id | SWS_FT_FI4 |
| 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_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:22223895 |
| Chain | Residue | Details |
| A | ALA2 | |
| B | ALA2 |
