1O9J
The X-ray crystal structure of eta-crystallin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001758 | molecular_function | retinal dehydrogenase activity |
| A | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| A | 0005198 | molecular_function | structural molecule activity |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 0018479 | molecular_function | benzaldehyde dehydrogenase (NAD+) activity |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0042574 | biological_process | retinal metabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0051287 | molecular_function | NAD binding |
| B | 0001758 | molecular_function | retinal dehydrogenase activity |
| B | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| B | 0005198 | molecular_function | structural molecule activity |
| B | 0005737 | cellular_component | cytoplasm |
| 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 | 0018479 | molecular_function | benzaldehyde dehydrogenase (NAD+) activity |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0042574 | biological_process | retinal metabolic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0051287 | molecular_function | NAD binding |
| C | 0001758 | molecular_function | retinal dehydrogenase activity |
| C | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| C | 0005198 | molecular_function | structural molecule activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006068 | biological_process | ethanol catabolic process |
| 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 | 0018479 | molecular_function | benzaldehyde dehydrogenase (NAD+) activity |
| C | 0032991 | cellular_component | protein-containing complex |
| C | 0042574 | biological_process | retinal metabolic process |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0051287 | molecular_function | NAD binding |
| D | 0001758 | molecular_function | retinal dehydrogenase activity |
| D | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| D | 0005198 | molecular_function | structural molecule activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006068 | biological_process | ethanol catabolic process |
| 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 | 0018479 | molecular_function | benzaldehyde dehydrogenase (NAD+) activity |
| D | 0032991 | cellular_component | protein-containing complex |
| D | 0042574 | biological_process | retinal metabolic process |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD A1501 |
| Chain | Residue |
| A | ILE165 |
| A | GLY229 |
| A | ALA230 |
| A | PHE243 |
| A | THR244 |
| A | GLY245 |
| A | SER246 |
| A | VAL249 |
| A | ILE253 |
| A | GLU268 |
| A | LEU269 |
| A | PHE166 |
| A | GLY270 |
| A | CYS302 |
| A | GLU399 |
| A | PHE401 |
| A | HOH2093 |
| A | HOH2094 |
| A | HOH2095 |
| A | PRO167 |
| A | TRP168 |
| A | ASN169 |
| A | LYS192 |
| A | ALA194 |
| A | GLU195 |
| A | GLY225 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE DTT B 900 |
| Chain | Residue |
| B | GLU195 |
| B | TYR224 |
| B | PRO226 |
| B | HOH2074 |
| B | HOH2082 |
| D | ALA348 |
| D | ASN351 |
| D | HOH2102 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD B1501 |
| Chain | Residue |
| B | ILE165 |
| B | PHE166 |
| B | PRO167 |
| B | TRP168 |
| B | ASN169 |
| B | LYS192 |
| B | ALA194 |
| B | GLU195 |
| B | GLY225 |
| B | GLY229 |
| B | ALA230 |
| B | PHE243 |
| B | THR244 |
| B | GLY245 |
| B | SER246 |
| B | VAL249 |
| B | ILE253 |
| B | GLU268 |
| B | LEU269 |
| B | GLY270 |
| B | CYS302 |
| B | GLU399 |
| B | PHE401 |
| B | HOH2143 |
| B | HOH2144 |
| B | HOH2145 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAD C1501 |
| Chain | Residue |
| C | ILE165 |
| C | PHE166 |
| C | PRO167 |
| C | TRP168 |
| C | ASN169 |
| C | LYS192 |
| C | ALA194 |
| C | GLU195 |
| C | GLY225 |
| C | GLY229 |
| C | ALA230 |
| C | PHE243 |
| C | THR244 |
| C | GLY245 |
| C | SER246 |
| C | VAL249 |
| C | ILE253 |
| C | GLU268 |
| C | LEU269 |
| C | CYS302 |
| C | GLU399 |
| C | PHE401 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DTU D 901 |
| Chain | Residue |
| B | ALA348 |
| B | ASN351 |
| D | GLU195 |
| D | TYR224 |
| D | HOH2065 |
| D | HOH2072 |
| site_id | AC6 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD D1501 |
| Chain | Residue |
| D | PHE243 |
| D | THR244 |
| D | GLY245 |
| D | SER246 |
| D | VAL249 |
| D | MET252 |
| D | GLU268 |
| D | LEU269 |
| D | GLY270 |
| D | CYS302 |
| D | GLU399 |
| D | PHE401 |
| D | LEU427 |
| D | HOH2077 |
| D | HOH2130 |
| D | ILE165 |
| D | PHE166 |
| D | PRO167 |
| D | TRP168 |
| D | ASN169 |
| D | LYS192 |
| D | ALA194 |
| D | GLU195 |
| D | GLY225 |
| D | GLY229 |
| D | ALA230 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FtNQGQSCIAAS |
| Chain | Residue | Details |
| A | PHE295-SER306 |
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:0000269|PubMed:12693930 |
| 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 |
| Chain | Residue | Details |
| A | ASN169 | |
| B | ASN169 | |
| C | ASN169 | |
| D | ASN169 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| A | CYS302 | |
| A | GLU268 | |
| A | ASN169 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| B | CYS302 | |
| B | GLU268 | |
| B | ASN169 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| C | CYS302 | |
| C | GLU268 | |
| C | ASN169 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| D | CYS302 | |
| D | GLU268 | |
| D | ASN169 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| A | CYS302 | |
| A | LYS192 | |
| A | GLU268 | |
| A | GLU399 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| B | CYS302 | |
| B | LYS192 | |
| B | GLU268 | |
| B | GLU399 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| C | CYS302 | |
| C | LYS192 | |
| C | GLU268 | |
| C | GLU399 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| D | CYS302 | |
| D | LYS192 | |
| D | GLU268 | |
| D | GLU399 |
