3AK4
Crystal structure of NADH-dependent quinuclidinone reductase from agrobacterium tumefaciens
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0006633 | biological_process | fatty acid biosynthetic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0048038 | molecular_function | quinone binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0006633 | biological_process | fatty acid biosynthetic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0048038 | molecular_function | quinone binding |
C | 0000166 | molecular_function | nucleotide binding |
C | 0006633 | biological_process | fatty acid biosynthetic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
C | 0048038 | molecular_function | quinone binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0006633 | biological_process | fatty acid biosynthetic process |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
D | 0048038 | molecular_function | quinone binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAD A 901 |
Chain | Residue |
A | GLY16 |
A | VAL64 |
A | ASN90 |
A | GLY92 |
A | THR141 |
A | ALA142 |
A | SER143 |
A | TYR156 |
A | LYS160 |
A | GLY187 |
A | VAL189 |
A | SER18 |
A | THR191 |
A | MET193 |
A | ARG196 |
A | HOH276 |
A | HOH281 |
A | HOH283 |
A | HOH291 |
A | HOH301 |
A | HOH413 |
A | LYS19 |
A | GLY20 |
A | ILE21 |
A | ASP40 |
A | LEU41 |
A | VAL62 |
A | ASP63 |
site_id | AC2 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAD B 902 |
Chain | Residue |
B | GLY16 |
B | LYS19 |
B | GLY20 |
B | ILE21 |
B | ASP40 |
B | LEU41 |
B | VAL62 |
B | ASP63 |
B | VAL64 |
B | ASN90 |
B | GLY92 |
B | THR141 |
B | ALA142 |
B | SER143 |
B | TYR156 |
B | LYS160 |
B | PRO186 |
B | GLY187 |
B | VAL189 |
B | THR191 |
B | MET193 |
B | ARG196 |
B | HOH282 |
B | HOH310 |
B | HOH333 |
B | HOH347 |
B | HOH404 |
site_id | AC3 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE NAD C 903 |
Chain | Residue |
C | GLY16 |
C | SER18 |
C | LYS19 |
C | GLY20 |
C | ILE21 |
C | ASP40 |
C | LEU41 |
C | VAL62 |
C | ASP63 |
C | VAL64 |
C | ASN90 |
C | ALA91 |
C | GLY92 |
C | THR141 |
C | ALA142 |
C | SER143 |
C | TYR156 |
C | LYS160 |
C | PRO186 |
C | GLY187 |
C | VAL189 |
C | THR191 |
C | MET193 |
C | ARG196 |
C | HOH267 |
C | HOH271 |
C | HOH274 |
C | HOH299 |
C | HOH302 |
C | HOH311 |
C | HOH490 |
site_id | AC4 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE NAD D 904 |
Chain | Residue |
D | THR141 |
D | ALA142 |
D | SER143 |
D | TYR156 |
D | LYS160 |
D | PRO186 |
D | GLY187 |
D | VAL189 |
D | THR191 |
D | MET193 |
D | ARG196 |
D | HOH280 |
D | HOH289 |
D | HOH304 |
D | HOH390 |
D | HOH661 |
D | GLY16 |
D | SER18 |
D | LYS19 |
D | GLY20 |
D | ILE21 |
D | ASP40 |
D | LEU41 |
D | VAL62 |
D | ASP63 |
D | VAL64 |
D | ASN90 |
D | ALA91 |
D | GLY92 |
Functional Information from PROSITE/UniProt
site_id | PS00061 |
Number of Residues | 29 |
Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SlaakvgaplLahYSASKFAVfGWTqALA |
Chain | Residue | Details |
A | SER143-ALA171 |