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 |