4E6P
Crystal structure of a probable sorbitol dehydrogenase (Target PSI-012078) from Sinorhizobium meliloti 1021
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003939 | molecular_function | L-iditol 2-dehydrogenase (NAD+) activity |
| 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 | 0003939 | molecular_function | L-iditol 2-dehydrogenase (NAD+) activity |
| 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 | 0003939 | molecular_function | L-iditol 2-dehydrogenase (NAD+) activity |
| 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 | 0003939 | molecular_function | L-iditol 2-dehydrogenase (NAD+) activity |
| 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 | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 301 |
| Chain | Residue |
| A | ALA47 |
| A | GLY51 |
| A | ALA54 |
| A | HOH444 |
| A | HOH457 |
| A | HOH468 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 302 |
| Chain | Residue |
| A | GLU147 |
| A | GLN141 |
| A | ALA142 |
| A | ARG145 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 303 |
| Chain | Residue |
| A | LYS2 |
| A | ARG3 |
| D | ARG3 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 301 |
| Chain | Residue |
| B | ALA47 |
| B | GLY51 |
| B | ALA54 |
| B | HOH421 |
| B | HOH479 |
| B | HOH495 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 302 |
| Chain | Residue |
| B | GLN141 |
| B | ALA142 |
| B | ARG145 |
| B | GLU147 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 303 |
| Chain | Residue |
| A | TYR104 |
| A | PHE108 |
| A | ALA109 |
| B | TYR104 |
| B | PHE108 |
| B | HOH503 |
| B | HOH508 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 304 |
| Chain | Residue |
| B | LYS7 |
| B | ASP82 |
| B | GLY133 |
| B | HOH445 |
| B | HOH496 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO B 305 |
| Chain | Residue |
| A | GLY143 |
| A | ARG144 |
| A | ARG145 |
| B | SER162 |
| B | GLN165 |
| B | EDO306 |
| B | HOH424 |
| B | HOH451 |
| B | HOH452 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 306 |
| Chain | Residue |
| A | GLN165 |
| B | GLY143 |
| B | ARG144 |
| B | ARG145 |
| B | EDO305 |
| B | HOH411 |
| B | HOH451 |
| B | HOH452 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 307 |
| Chain | Residue |
| B | VAL75 |
| B | GLN125 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA C 301 |
| Chain | Residue |
| C | ALA47 |
| C | GLY51 |
| C | ALA54 |
| C | HOH492 |
| C | HOH497 |
| C | HOH512 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO C 302 |
| Chain | Residue |
| C | TYR104 |
| C | PHE108 |
| C | ALA109 |
| C | HOH469 |
| D | TYR104 |
| D | GLU105 |
| D | PHE108 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 303 |
| Chain | Residue |
| C | ARG16 |
| C | ASP39 |
| C | GLU41 |
| C | ARG42 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C 304 |
| Chain | Residue |
| C | LYS7 |
| C | ASP82 |
| C | GLY133 |
| C | HOH485 |
| C | HOH490 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO C 305 |
| Chain | Residue |
| C | SER8 |
| C | ALA78 |
| C | GLY80 |
| C | LEU81 |
| C | ASP82 |
| C | GLN129 |
| C | ARG131 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA D 301 |
| Chain | Residue |
| D | ALA47 |
| D | GLY51 |
| D | ALA54 |
| D | EDO304 |
| D | HOH415 |
| site_id | BC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EDO D 302 |
| Chain | Residue |
| D | ASP92 |
| D | LEU93 |
| D | ALA94 |
| D | ILE99 |
| D | LEU149 |
| D | VAL150 |
| D | ALA151 |
| D | ILE152 |
| D | TYR153 |
| D | HOH426 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 303 |
| Chain | Residue |
| D | GLY253 |
| D | ASN254 |
| D | TRP255 |
| D | HOH437 |
| D | PRO218 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO D 304 |
| Chain | Residue |
| B | GLY6 |
| D | ALA47 |
| D | PRO52 |
| D | ALA54 |
| D | NA301 |
| D | HOH444 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 305 |
| Chain | Residue |
| C | ILE99 |
| C | ARG101 |
| D | GLN64 |
| D | GLN120 |
| D | ARG124 |
| site_id | CC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 306 |
| Chain | Residue |
| C | SER162 |
| C | GLN165 |
| C | HOH418 |
| D | GLY143 |
| D | ARG144 |
| D | ARG145 |
| D | HOH448 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SqagrrgealVaiYCATKAAViSLTqSAG |
| Chain | Residue | Details |
| A | SER140-GLY168 |
