7MJC
Crystal Structure Analysis of ALDH1B1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0005829 | cellular_component | cytosol |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0006068 | biological_process | ethanol catabolic process |
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 | 0051287 | molecular_function | NAD binding |
B | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0005829 | cellular_component | cytosol |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0006068 | biological_process | ethanol catabolic process |
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 | 0051287 | molecular_function | NAD binding |
Functional Information from PROSITE/UniProt
site_id | PS00070 |
Number of Residues | 12 |
Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfNMGQCCCAGS |
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 | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008 |
Chain | Residue | Details |
A | GLU268 | |
B | GLU268 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008 |
Chain | Residue | Details |
A | CYS302 | |
B | CYS302 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLY245 | |
B | GLY245 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0000250 |
Chain | Residue | Details |
A | ASN169 | |
B | ASN169 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9CZS1 |
Chain | Residue | Details |
A | LYS34 | |
A | LYS412 | |
B | LYS34 | |
B | LYS412 |
site_id | SWS_FT_FI6 |
Number of Residues | 12 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CZS1 |
Chain | Residue | Details |
A | LYS35 | |
B | LYS382 | |
B | LYS397 | |
B | LYS409 | |
A | LYS347 | |
A | LYS366 | |
A | LYS382 | |
A | LYS397 | |
A | LYS409 | |
B | LYS35 | |
B | LYS347 | |
B | LYS366 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9CZS1 |
Chain | Residue | Details |
A | LYS64 | |
B | LYS64 |