Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016491 | molecular_function | oxidoreductase activity |
B | 0016491 | molecular_function | oxidoreductase activity |
C | 0016491 | molecular_function | oxidoreductase activity |
D | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE NAP A 269 |
Chain | Residue |
A | ARG14 |
A | THR64 |
A | ASN93 |
A | ALA94 |
A | SER95 |
A | THR126 |
A | LEU159 |
A | CYS160 |
A | TYR174 |
A | LYS178 |
A | PRO204 |
A | ILE15 |
A | GLY205 |
A | VAL206 |
A | SER207 |
A | LEU208 |
A | JU2270 |
A | HOH276 |
A | HOH284 |
A | HOH292 |
A | HOH361 |
A | HOH370 |
A | TYR34 |
A | HOH406 |
A | HOH435 |
A | HOH574 |
A | HIS35 |
A | ASN36 |
A | SER37 |
A | ALA61 |
A | ASP62 |
A | LEU63 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE JU2 A 270 |
Chain | Residue |
A | ARG14 |
A | SER95 |
A | PHE97 |
A | TYR174 |
A | PRO210 |
A | NAP269 |
A | HOH361 |
A | HOH547 |
site_id | AC3 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE NAP B 269 |
Chain | Residue |
B | ARG14 |
B | ILE15 |
B | HIS33 |
B | TYR34 |
B | HIS35 |
B | ASN36 |
B | SER37 |
B | ALA61 |
B | ASP62 |
B | LEU63 |
B | THR64 |
B | ASN93 |
B | ALA94 |
B | SER95 |
B | THR126 |
B | LEU159 |
B | CYS160 |
B | TYR174 |
B | LYS178 |
B | PRO204 |
B | GLY205 |
B | SER207 |
B | LEU208 |
B | JU2270 |
B | HOH277 |
B | HOH292 |
B | HOH300 |
B | HOH312 |
B | HOH419 |
B | HOH458 |
B | HOH467 |
B | HOH518 |
B | HOH537 |
B | HOH694 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE JU2 B 270 |
Chain | Residue |
B | ARG14 |
B | SER95 |
B | PHE97 |
B | ASP161 |
B | TYR174 |
B | PRO210 |
B | NAP269 |
B | HOH300 |
site_id | AC5 |
Number of Residues | 33 |
Details | BINDING SITE FOR RESIDUE NAP C 269 |
Chain | Residue |
C | LYS178 |
C | PRO204 |
C | GLY205 |
C | VAL206 |
C | SER207 |
C | LEU208 |
C | JU2270 |
C | HOH271 |
C | HOH273 |
C | HOH276 |
C | HOH289 |
C | HOH314 |
C | HOH346 |
C | HOH506 |
C | HOH532 |
C | HOH669 |
C | ARG14 |
C | ILE15 |
C | TYR34 |
C | HIS35 |
C | ASN36 |
C | SER37 |
C | ALA61 |
C | ASP62 |
C | LEU63 |
C | THR64 |
C | ASN93 |
C | ALA94 |
C | SER95 |
C | THR126 |
C | LEU159 |
C | CYS160 |
C | TYR174 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE JU2 C 270 |
Chain | Residue |
C | ARG14 |
C | SER95 |
C | PHE97 |
C | ASP161 |
C | TYR174 |
C | PRO210 |
C | NAP269 |
C | HOH314 |
site_id | AC7 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE NAP D 269 |
Chain | Residue |
D | ARG14 |
D | ILE15 |
D | TYR34 |
D | HIS35 |
D | ASN36 |
D | SER37 |
D | ALA61 |
D | ASP62 |
D | LEU63 |
D | THR64 |
D | ASN93 |
D | ALA94 |
D | SER95 |
D | THR126 |
D | LEU159 |
D | CYS160 |
D | TYR174 |
D | LYS178 |
D | PRO204 |
D | GLY205 |
D | VAL206 |
D | SER207 |
D | LEU208 |
D | JU2270 |
D | HOH300 |
D | HOH308 |
D | HOH323 |
D | HOH333 |
D | HOH339 |
D | HOH345 |
D | HOH684 |
D | HOH688 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE JU2 D 270 |
Chain | Residue |
D | ARG14 |
D | SER95 |
D | PHE97 |
D | TYR174 |
D | PRO210 |
D | NAP269 |
D | HOH339 |
Functional Information from PROSITE/UniProt
site_id | PS00061 |
Number of Residues | 29 |
Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. DamvdqpcmaFslYNMGKHALvGLTqSAA |
Chain | Residue | Details |
A | ASP161-ALA189 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
A | ASP165 | |
site_id | CSA10 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
B | PHE171 | |
B | LYS178 | |
site_id | CSA11 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
C | PHE171 | |
C | LYS178 | |
site_id | CSA12 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
D | PHE171 | |
D | LYS178 | |
site_id | CSA13 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
A | TYR174 | |
A | LYS178 | |
site_id | CSA14 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
B | TYR174 | |
B | LYS178 | |
site_id | CSA15 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
C | TYR174 | |
C | LYS178 | |
site_id | CSA16 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
D | TYR174 | |
D | LYS178 | |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
B | ASP165 | |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
C | ASP165 | |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
D | ASP165 | |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
A | SER152 | |
A | TYR174 | |
A | LYS178 | |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
B | SER152 | |
B | TYR174 | |
B | LYS178 | |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
C | SER152 | |
C | TYR174 | |
C | LYS178 | |
site_id | CSA8 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
D | SER152 | |
D | TYR174 | |
D | LYS178 | |
site_id | CSA9 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
A | PHE171 | |
A | LYS178 | |