4FQF
Crystal structure of a thionitrate intermediate of human aldehyde dehydrogenase-2
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
A | 0004030 | molecular_function | aldehyde dehydrogenase [NAD(P)+] activity |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0006066 | biological_process | alcohol metabolic process |
A | 0006068 | biological_process | ethanol catabolic process |
A | 0008957 | molecular_function | phenylacetaldehyde dehydrogenase activity |
A | 0009055 | molecular_function | electron transfer activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
A | 0018547 | molecular_function | nitroglycerin reductase activity |
A | 0043878 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity |
A | 0046185 | biological_process | aldehyde catabolic process |
A | 0051287 | molecular_function | NAD binding |
A | 0070062 | cellular_component | extracellular exosome |
A | 0106435 | molecular_function | carboxylesterase activity |
A | 1903179 | biological_process | regulation of dopamine biosynthetic process |
A | 1905627 | biological_process | regulation of serotonin biosynthetic process |
B | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
B | 0004030 | molecular_function | aldehyde dehydrogenase [NAD(P)+] activity |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0006066 | biological_process | alcohol metabolic process |
B | 0006068 | biological_process | ethanol catabolic process |
B | 0008957 | molecular_function | phenylacetaldehyde dehydrogenase activity |
B | 0009055 | molecular_function | electron transfer activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
B | 0018547 | molecular_function | nitroglycerin reductase activity |
B | 0043878 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity |
B | 0046185 | biological_process | aldehyde catabolic process |
B | 0051287 | molecular_function | NAD binding |
B | 0070062 | cellular_component | extracellular exosome |
B | 0106435 | molecular_function | carboxylesterase activity |
B | 1903179 | biological_process | regulation of dopamine biosynthetic process |
B | 1905627 | biological_process | regulation of serotonin biosynthetic process |
C | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
C | 0004030 | molecular_function | aldehyde dehydrogenase [NAD(P)+] activity |
C | 0005739 | cellular_component | mitochondrion |
C | 0005759 | cellular_component | mitochondrial matrix |
C | 0005975 | biological_process | carbohydrate metabolic process |
C | 0006066 | biological_process | alcohol metabolic process |
C | 0006068 | biological_process | ethanol catabolic process |
C | 0008957 | molecular_function | phenylacetaldehyde dehydrogenase activity |
C | 0009055 | molecular_function | electron transfer activity |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
C | 0018547 | molecular_function | nitroglycerin reductase activity |
C | 0043878 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity |
C | 0046185 | biological_process | aldehyde catabolic process |
C | 0051287 | molecular_function | NAD binding |
C | 0070062 | cellular_component | extracellular exosome |
C | 0106435 | molecular_function | carboxylesterase activity |
C | 1903179 | biological_process | regulation of dopamine biosynthetic process |
C | 1905627 | biological_process | regulation of serotonin biosynthetic process |
D | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
D | 0004030 | molecular_function | aldehyde dehydrogenase [NAD(P)+] activity |
D | 0005739 | cellular_component | mitochondrion |
D | 0005759 | cellular_component | mitochondrial matrix |
D | 0005975 | biological_process | carbohydrate metabolic process |
D | 0006066 | biological_process | alcohol metabolic process |
D | 0006068 | biological_process | ethanol catabolic process |
D | 0008957 | molecular_function | phenylacetaldehyde dehydrogenase activity |
D | 0009055 | molecular_function | electron transfer activity |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
D | 0018547 | molecular_function | nitroglycerin reductase activity |
D | 0043878 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity |
D | 0046185 | biological_process | aldehyde catabolic process |
D | 0051287 | molecular_function | NAD binding |
D | 0070062 | cellular_component | extracellular exosome |
D | 0106435 | molecular_function | carboxylesterase activity |
D | 1903179 | biological_process | regulation of dopamine biosynthetic process |
D | 1905627 | biological_process | regulation of serotonin biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE 2NO A 701 |
Chain | Residue |
A | ASN169 |
A | CYS302 |
A | NAD702 |
site_id | AC2 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAD A 702 |
Chain | Residue |
A | ALA194 |
A | GLU195 |
A | GLY225 |
A | GLY229 |
A | ALA230 |
A | PHE243 |
A | GLY245 |
A | SER246 |
A | ILE249 |
A | LEU269 |
A | CYS302 |
A | GLN349 |
A | LYS352 |
A | GLU399 |
A | 2NO701 |
A | MG703 |
A | HOH817 |
A | HOH907 |
A | HOH924 |
A | HOH946 |
A | HOH1018 |
A | ILE165 |
A | ILE166 |
A | PRO167 |
A | TRP168 |
A | ASN169 |
A | LYS192 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MG A 703 |
Chain | Residue |
A | NAD702 |
A | HOH1018 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE URE A 704 |
Chain | Residue |
A | GLU157 |
A | PRO158 |
A | VAL159 |
A | HOH1022 |
B | GLN447 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 705 |
Chain | Residue |
A | THR39 |
A | VAL40 |
A | ASP109 |
A | GLN196 |
A | HOH816 |
A | HOH827 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE URE A 706 |
Chain | Residue |
A | PHE151 |
C | ASN440 |
C | SER443 |
D | TYR153 |
D | ARG155 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE URE B 701 |
Chain | Residue |
A | ASN440 |
A | SER443 |
B | TYR153 |
B | ARG155 |
C | PHE151 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE 2NO B 702 |
Chain | Residue |
B | ASN169 |
B | CYS302 |
B | NAD703 |
site_id | AC9 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE NAD B 703 |
Chain | Residue |
B | ILE165 |
B | ILE166 |
B | PRO167 |
B | TRP168 |
B | ASN169 |
B | LYS192 |
B | ALA194 |
B | GLU195 |
B | GLY225 |
B | GLY229 |
B | ALA230 |
B | PHE243 |
B | GLY245 |
B | SER246 |
B | ILE249 |
B | LEU269 |
B | CYS302 |
B | GLN349 |
B | LYS352 |
B | GLU399 |
B | PHE401 |
B | 2NO702 |
B | MG704 |
B | HOH2182 |
B | HOH2197 |
B | HOH2210 |
B | HOH2223 |
B | HOH2226 |
B | HOH2236 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG B 704 |
Chain | Residue |
B | NAD703 |
B | HOH2197 |
B | HOH2226 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE URE B 705 |
Chain | Residue |
A | GLN447 |
B | GLU157 |
B | PRO158 |
B | VAL159 |
B | HOH2344 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA B 706 |
Chain | Residue |
B | THR39 |
B | VAL40 |
B | ASP109 |
B | GLN196 |
B | HOH2353 |
B | HOH2354 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE 2NO C 701 |
Chain | Residue |
C | ASN169 |
C | CYS302 |
C | NAD703 |
C | HOH996 |
site_id | BC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MG C 702 |
Chain | Residue |
C | NAD703 |
site_id | BC6 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAD C 703 |
Chain | Residue |
C | ILE165 |
C | ILE166 |
C | PRO167 |
C | TRP168 |
C | ASN169 |
C | LYS192 |
C | ALA194 |
C | GLU195 |
C | GLY225 |
C | GLY229 |
C | ALA230 |
C | PHE243 |
C | GLY245 |
C | SER246 |
C | ILE249 |
C | LEU269 |
C | CYS302 |
C | GLN349 |
C | LYS352 |
C | GLU399 |
C | PHE401 |
C | 2NO701 |
C | MG702 |
C | HOH831 |
C | HOH922 |
C | HOH925 |
C | HOH997 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE URE C 704 |
Chain | Residue |
C | GLU157 |
C | PRO158 |
C | VAL159 |
C | HOH964 |
D | GLN447 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA C 705 |
Chain | Residue |
C | THR39 |
C | VAL40 |
C | ASP109 |
C | GLN196 |
C | HOH934 |
site_id | BC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE 2NO D 701 |
Chain | Residue |
D | ASN169 |
D | CYS302 |
D | NAD702 |
site_id | CC1 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE NAD D 702 |
Chain | Residue |
D | ILE165 |
D | ILE166 |
D | PRO167 |
D | TRP168 |
D | ASN169 |
D | LYS192 |
D | ALA194 |
D | GLU195 |
D | GLN196 |
D | GLY225 |
D | GLY229 |
D | ALA230 |
D | PHE243 |
D | GLY245 |
D | SER246 |
D | ILE249 |
D | LEU269 |
D | CYS302 |
D | GLN349 |
D | GLU399 |
D | 2NO701 |
D | MG703 |
D | HOH876 |
D | HOH907 |
D | HOH948 |
D | HOH953 |
site_id | CC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MG D 703 |
Chain | Residue |
D | NAD702 |
site_id | CC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE URE D 704 |
Chain | Residue |
C | GLN447 |
D | PHE70 |
D | GLU157 |
D | PRO158 |
D | VAL159 |
D | HOH975 |
site_id | CC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA D 705 |
Chain | Residue |
D | THR39 |
D | VAL40 |
D | ASP109 |
D | GLN196 |
D | HOH918 |
D | HOH926 |
Functional Information from PROSITE/UniProt
site_id | PS00070 |
Number of Residues | 12 |
Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfNQGQCCCAGS |
Chain | Residue | Details |
A | PHE295-SER306 |
site_id | PS00687 |
Number of Residues | 8 |
Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP |
Chain | Residue | Details |
A | LEU267-PRO274 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | GLU268 | |
B | GLU268 | |
C | GLU268 | |
D | GLU268 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Nucleophile |
Chain | Residue | Details |
A | CYS302 | |
B | CYS302 | |
C | CYS302 | |
D | CYS302 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLY245 | |
B | GLY245 | |
C | GLY245 | |
D | GLY245 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P20000 |
Chain | Residue | Details |
A | ASN169 | |
B | ASN169 | |
C | ASN169 | |
D | ASN169 |
site_id | SWS_FT_FI5 |
Number of Residues | 36 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P47738 |
Chain | Residue | Details |
A | LYS35 | |
B | LYS35 | |
B | LYS56 | |
B | LYS61 | |
B | LYS142 | |
B | LYS351 | |
B | LYS366 | |
B | LYS409 | |
B | LYS411 | |
B | LYS434 | |
C | LYS35 | |
A | LYS56 | |
C | LYS56 | |
C | LYS61 | |
C | LYS142 | |
C | LYS351 | |
C | LYS366 | |
C | LYS409 | |
C | LYS411 | |
C | LYS434 | |
D | LYS35 | |
D | LYS56 | |
A | LYS61 | |
D | LYS61 | |
D | LYS142 | |
D | LYS351 | |
D | LYS366 | |
D | LYS409 | |
D | LYS411 | |
D | LYS434 | |
A | LYS142 | |
A | LYS351 | |
A | LYS366 | |
A | LYS409 | |
A | LYS411 | |
A | LYS434 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 803 |
Chain | Residue | Details |
A | LYS192 | electrostatic stabiliser |
A | GLU268 | electrostatic stabiliser, proton acceptor, proton donor |
A | CYS302 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
A | GLU399 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 803 |
Chain | Residue | Details |
B | LYS192 | electrostatic stabiliser |
B | GLU268 | electrostatic stabiliser, proton acceptor, proton donor |
B | CYS302 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
B | GLU399 | electrostatic stabiliser |
site_id | MCSA3 |
Number of Residues | 4 |
Details | M-CSA 803 |
Chain | Residue | Details |
C | LYS192 | electrostatic stabiliser |
C | GLU268 | electrostatic stabiliser, proton acceptor, proton donor |
C | CYS302 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
C | GLU399 | electrostatic stabiliser |
site_id | MCSA4 |
Number of Residues | 4 |
Details | M-CSA 803 |
Chain | Residue | Details |
D | LYS192 | electrostatic stabiliser |
D | GLU268 | electrostatic stabiliser, proton acceptor, proton donor |
D | CYS302 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
D | GLU399 | electrostatic stabiliser |