3QJ5
S-nitrosoglutathione reductase (GSNOR) in complex with N6022
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| A | 0005504 | molecular_function | fatty acid binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0010430 | biological_process | fatty acid omega-oxidation |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0018467 | molecular_function | formaldehyde dehydrogenase (NAD+) activity |
| A | 0044281 | biological_process | small molecule metabolic process |
| A | 0046294 | biological_process | formaldehyde catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051775 | biological_process | response to redox state |
| A | 0051903 | molecular_function | S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity |
| A | 0070062 | cellular_component | extracellular exosome |
| 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 | 0005504 | molecular_function | fatty acid binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0010430 | biological_process | fatty acid omega-oxidation |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0018467 | molecular_function | formaldehyde dehydrogenase (NAD+) activity |
| B | 0044281 | biological_process | small molecule metabolic process |
| B | 0046294 | biological_process | formaldehyde catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051775 | biological_process | response to redox state |
| B | 0051903 | molecular_function | S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity |
| B | 0070062 | cellular_component | extracellular exosome |
| 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 375 |
| Chain | Residue |
| A | CYS96 |
| A | CYS99 |
| A | CYS102 |
| A | CYS110 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 376 |
| Chain | Residue |
| A | CYS44 |
| A | HIS66 |
| A | CYS173 |
| A | 022374 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 375 |
| Chain | Residue |
| B | CYS99 |
| B | CYS102 |
| B | CYS110 |
| B | CYS96 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 376 |
| Chain | Residue |
| B | CYS44 |
| B | HIS66 |
| B | CYS173 |
| B | 022377 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 501 |
| Chain | Residue |
| A | HOH456 |
| A | HOH626 |
| B | ALA186 |
| B | LYS187 |
| B | GLU189 |
| B | TYR263 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 602 |
| Chain | Residue |
| A | ALA186 |
| A | LYS187 |
| A | GLU189 |
| A | TYR263 |
| A | HOH581 |
| A | HOH691 |
| site_id | AC7 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAD A 500 |
| Chain | Residue |
| A | HIS45 |
| A | CYS173 |
| A | THR177 |
| A | GLY198 |
| A | GLY200 |
| A | GLY201 |
| A | VAL202 |
| A | ASP222 |
| A | ILE223 |
| A | CYS267 |
| A | ILE268 |
| A | VAL273 |
| A | VAL291 |
| A | VAL293 |
| A | THR316 |
| A | ALA317 |
| A | PHE318 |
| A | ARG368 |
| A | 022374 |
| A | N2P379 |
| A | HOH384 |
| A | HOH391 |
| A | HOH394 |
| A | HOH420 |
| A | HOH467 |
| A | HOH468 |
| A | HOH481 |
| A | HOH525 |
| A | HOH577 |
| A | HOH609 |
| A | HOH635 |
| A | HOH637 |
| A | HOH679 |
| site_id | AC8 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAD B 374 |
| Chain | Residue |
| B | HIS45 |
| B | CYS173 |
| B | THR177 |
| B | GLY198 |
| B | GLY200 |
| B | GLY201 |
| B | VAL202 |
| B | ASP222 |
| B | ILE223 |
| B | CYS267 |
| B | ILE268 |
| B | VAL273 |
| B | VAL291 |
| B | GLY292 |
| B | VAL293 |
| B | THR316 |
| B | ALA317 |
| B | PHE318 |
| B | ARG368 |
| B | 022377 |
| B | N2P379 |
| B | HOH431 |
| B | HOH437 |
| B | HOH465 |
| B | HOH483 |
| B | HOH495 |
| B | HOH498 |
| B | HOH518 |
| B | HOH536 |
| B | HOH553 |
| B | HOH559 |
| B | HOH631 |
| B | HOH753 |
| site_id | AC9 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE 022 A 374 |
| Chain | Residue |
| A | GLN111 |
| A | ARG114 |
| A | GLN117 |
| A | MET140 |
| A | CYS173 |
| A | ZN376 |
| A | HOH427 |
| A | NAD500 |
| A | HOH565 |
| A | HOH601 |
| B | LYS283 |
| B | VAL308 |
| B | THR309 |
| A | CYS44 |
| A | THR46 |
| A | HIS66 |
| A | TYR92 |
| A | ILE93 |
| site_id | BC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 022 B 377 |
| Chain | Residue |
| A | LYS283 |
| A | THR309 |
| B | CYS44 |
| B | THR46 |
| B | HIS66 |
| B | TYR92 |
| B | ILE93 |
| B | GLN111 |
| B | ARG114 |
| B | GLN117 |
| B | MET140 |
| B | CYS173 |
| B | NAD374 |
| B | ZN376 |
| B | HOH411 |
| B | HOH503 |
| B | HOH647 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 1PE B 378 |
| Chain | Residue |
| B | LYS81 |
| B | GLN95 |
| B | CYS96 |
| B | VAL324 |
| B | GLU325 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 1PE A 377 |
| Chain | Residue |
| A | LYS6 |
| A | CYS7 |
| A | GLU147 |
| A | TYR148 |
| A | HOH469 |
| B | TYR334 |
| B | MET335 |
| B | LYS337 |
| B | ASP342 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 1PE A 378 |
| Chain | Residue |
| A | LYS81 |
| A | GLN95 |
| A | CYS96 |
| A | GLY97 |
| A | HOH413 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE N2P B 379 |
| Chain | Residue |
| B | HIS45 |
| B | THR46 |
| B | TYR49 |
| B | VAL293 |
| B | ALA295 |
| B | NAD374 |
| B | HOH715 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE N2P B 380 |
| Chain | Residue |
| A | THR135 |
| B | GLN243 |
| B | ASP244 |
| B | SER246 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE N2P A 379 |
| Chain | Residue |
| A | HIS45 |
| A | TYR49 |
| A | VAL293 |
| A | ALA295 |
| A | NAD500 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE TRS A 380 |
| Chain | Residue |
| A | LYS314 |
| A | HOH626 |
| A | HOH691 |
| B | LYS314 |
Functional Information from PROSITE/UniProt
| site_id | PS00059 |
| Number of Residues | 15 |
| Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEgAGIvesvGegV |
| Chain | Residue | Details |
| A | GLY65-VAL79 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"3365377","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for FDH activity and activation by fatty acids","evidences":[{"source":"PubMed","id":"8460164","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8494891","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P28474","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 12 |
| Details | M-CSA 464 |
| Chain | Residue | Details |
| A | CYS44 | metal ligand |
| A | ARG114 | activator |
| A | CYS173 | metal ligand |
| A | ARG368 | steric role |
| A | HIS45 | proton shuttle (general acid/base) |
| A | THR46 | proton shuttle (general acid/base) |
| A | HIS66 | metal ligand |
| A | GLU67 | metal ligand |
| A | CYS96 | metal ligand |
| A | CYS99 | metal ligand |
| A | CYS102 | metal ligand |
| A | CYS110 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 12 |
| Details | M-CSA 464 |
| Chain | Residue | Details |
| B | CYS44 | metal ligand |
| B | ARG114 | activator |
| B | CYS173 | metal ligand |
| B | ARG368 | steric role |
| B | HIS45 | proton shuttle (general acid/base) |
| B | THR46 | proton shuttle (general acid/base) |
| B | HIS66 | metal ligand |
| B | GLU67 | metal ligand |
| B | CYS96 | metal ligand |
| B | CYS99 | metal ligand |
| B | CYS102 | metal ligand |
| B | CYS110 | metal ligand |
