Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003723 | molecular_function | RNA binding |
A | 0003730 | molecular_function | mRNA 3'-UTR binding |
A | 0003960 | molecular_function | NADPH:quinone reductase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0007601 | biological_process | visual perception |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0042178 | biological_process | xenobiotic catabolic process |
A | 0042802 | molecular_function | identical protein binding |
A | 0051289 | biological_process | protein homotetramerization |
A | 0070062 | cellular_component | extracellular exosome |
A | 0070402 | molecular_function | NADPH binding |
A | 0070404 | molecular_function | NADH binding |
B | 0003723 | molecular_function | RNA binding |
B | 0003730 | molecular_function | mRNA 3'-UTR binding |
B | 0003960 | molecular_function | NADPH:quinone reductase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0007601 | biological_process | visual perception |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0042178 | biological_process | xenobiotic catabolic process |
B | 0042802 | molecular_function | identical protein binding |
B | 0051289 | biological_process | protein homotetramerization |
B | 0070062 | cellular_component | extracellular exosome |
B | 0070402 | molecular_function | NADPH binding |
B | 0070404 | molecular_function | NADH binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACT B 811 |
Chain | Residue |
A | VAL50 |
A | TYR53 |
A | TYR59 |
A | NAP801 |
A | HOH986 |
B | ARG257 |
B | MET260 |
B | HOH822 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACT A 812 |
Chain | Residue |
A | MET260 |
A | HOH824 |
B | VAL50 |
B | TYR53 |
B | TYR59 |
B | NAP802 |
B | HOH950 |
A | ARG257 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT A 813 |
Chain | Residue |
A | VAL80 |
A | ASP82 |
A | HOH1154 |
B | VAL80 |
B | GLY81 |
B | ASP82 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 816 |
Chain | Residue |
A | GLY156 |
A | GLY159 |
A | GLY160 |
A | GLY162 |
A | NAP801 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL B 817 |
Chain | Residue |
B | GLY156 |
B | GLY159 |
B | GLY160 |
B | GLY162 |
B | NAP802 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL A 818 |
Chain | Residue |
A | SER97 |
A | THR98 |
A | ALA109 |
A | ALA110 |
A | THR113 |
A | HOH870 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL B 819 |
Chain | Residue |
B | GLU51 |
B | PRO69 |
B | GLY70 |
B | HOH864 |
B | HOH924 |
B | HOH1155 |
site_id | AC8 |
Number of Residues | 38 |
Details | BINDING SITE FOR RESIDUE NAP A 801 |
Chain | Residue |
A | PRO49 |
A | TYR53 |
A | ILE131 |
A | THR135 |
A | HIS155 |
A | GLY156 |
A | SER158 |
A | GLY159 |
A | GLY160 |
A | VAL161 |
A | ALA180 |
A | GLY181 |
A | HIS200 |
A | LEU225 |
A | ASN229 |
A | VAL246 |
A | ARG249 |
A | VAL269 |
A | THR270 |
A | LEU271 |
A | ILE315 |
A | GLY320 |
A | ALA321 |
A | CL816 |
A | HOH833 |
A | HOH834 |
A | HOH835 |
A | HOH906 |
A | HOH907 |
A | HOH908 |
A | HOH909 |
A | HOH910 |
A | HOH937 |
A | HOH938 |
A | HOH944 |
A | HOH1073 |
B | ACT811 |
B | HOH822 |
site_id | AC9 |
Number of Residues | 42 |
Details | BINDING SITE FOR RESIDUE NAP B 802 |
Chain | Residue |
B | VAL246 |
B | GLY247 |
B | ARG249 |
B | VAL269 |
B | THR270 |
B | LEU271 |
B | ILE315 |
B | GLY320 |
B | ALA321 |
B | CL817 |
B | HOH825 |
B | HOH867 |
B | HOH898 |
B | HOH899 |
B | HOH900 |
B | HOH902 |
B | HOH903 |
B | HOH905 |
B | HOH906 |
B | HOH938 |
B | HOH944 |
B | HOH949 |
B | HOH950 |
B | HOH1060 |
B | HOH1063 |
A | ACT812 |
A | HOH824 |
B | PRO49 |
B | TYR53 |
B | ILE131 |
B | THR135 |
B | HIS155 |
B | GLY156 |
B | SER158 |
B | GLY159 |
B | GLY160 |
B | VAL161 |
B | ALA180 |
B | GLY181 |
B | HIS200 |
B | LEU225 |
B | ASN229 |
site_id | BC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 814 |
Chain | Residue |
A | ALA171 |
A | TYR172 |
A | ILE292 |
A | TRP294 |
A | HOH962 |
A | HOH963 |
B | ALA171 |
B | TYR172 |
B | TRP294 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 815 |
Chain | Residue |
A | ASP82 |
A | ASN83 |
A | SER85 |
A | HOH866 |
A | HOH1152 |
B | LYS34 |
site_id | BC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 820 |
Chain | Residue |
A | SER301 |
A | TYR303 |
A | ASN314 |
A | SER319 |
A | GLY320 |
A | MET325 |
A | HOH828 |
A | HOH840 |
A | HOH1041 |
A | HOH1131 |
site_id | BC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL B 821 |
Chain | Residue |
B | SER301 |
B | TYR303 |
B | ASN314 |
B | GLY318 |
B | SER319 |
B | GLY320 |
B | MET325 |
B | HOH834 |
B | HOH897 |
B | HOH1156 |
Functional Information from PROSITE/UniProt
site_id | PS01162 |
Number of Residues | 22 |
Details | QOR_ZETA_CRYSTAL Quinone oxidoreductase / zeta-crystallin signature. GEsvLvhgASGGvGlaacQiaR |
Chain | Residue | Details |
A | GLY149-ARG170 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000269|Ref.17 |
Chain | Residue | Details |
A | VAL269 | |
B | TYR53 | |
B | SER158 | |
B | GLY181 | |
B | HIS200 | |
B | ASN229 | |
B | VAL246 | |
B | VAL269 | |
A | TYR53 | |
A | SER158 | |
A | GLY181 | |
A | HIS200 | |
A | ASN229 | |
A | VAL246 | |
Chain | Residue | Details |
A | ALA2 | |
B | ALA2 | |
Chain | Residue | Details |
A | LYS23 | |
B | LYS23 | |
Chain | Residue | Details |
A | SER248 | |
B | SER248 | |
Chain | Residue | Details |
A | LYS296 | |
B | LYS296 | |