3QJ5
S-nitrosoglutathione reductase (GSNOR) in complex with N6022
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001523 | biological_process | retinoid metabolic process |
A | 0003016 | biological_process | respiratory system process |
A | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
A | 0004024 | molecular_function | alcohol dehydrogenase (NAD+) activity, zinc-dependent |
A | 0005504 | molecular_function | fatty acid binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
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 | 0032496 | biological_process | response to lipopolysaccharide |
A | 0042802 | molecular_function | identical protein binding |
A | 0044281 | biological_process | small molecule metabolic process |
A | 0045777 | biological_process | positive regulation of blood pressure |
A | 0046294 | biological_process | formaldehyde catabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0051409 | biological_process | response to nitrosative stress |
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 | 0106321 | molecular_function | S-(hydroxymethyl)glutathione dehydrogenase (NADP+) activity |
A | 0106322 | molecular_function | S-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity |
B | 0001523 | biological_process | retinoid metabolic process |
B | 0003016 | biological_process | respiratory system process |
B | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
B | 0004024 | molecular_function | alcohol dehydrogenase (NAD+) activity, zinc-dependent |
B | 0005504 | molecular_function | fatty acid binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
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 | 0032496 | biological_process | response to lipopolysaccharide |
B | 0042802 | molecular_function | identical protein binding |
B | 0044281 | biological_process | small molecule metabolic process |
B | 0045777 | biological_process | positive regulation of blood pressure |
B | 0046294 | biological_process | formaldehyde catabolic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0051409 | biological_process | response to nitrosative stress |
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 | 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: BINDING => ECO:0000269|PubMed:3365377 |
Chain | Residue | Details |
A | CYS44 | |
B | CYS96 | |
B | CYS99 | |
B | CYS102 | |
B | CYS110 | |
B | CYS173 | |
A | HIS66 | |
A | CYS96 | |
A | CYS99 | |
A | CYS102 | |
A | CYS110 | |
A | CYS173 | |
B | CYS44 | |
B | HIS66 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Important for FDH activity and activation by fatty acids => ECO:0000269|PubMed:8460164, ECO:0000269|PubMed:8494891 |
Chain | Residue | Details |
A | ARG114 | |
B | ARG114 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330 |
Chain | Residue | Details |
A | ALA1 | |
B | ALA1 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P28474 |
Chain | Residue | Details |
A | LYS232 | |
A | LYS314 | |
B | LYS232 | |
B | LYS314 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER246 | |
B | SER246 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER323 | |
A | SER350 | |
B | SER323 | |
B | SER350 |
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 |