7KRM
Putative FabG bound to NADH from Acinetobacter baumannii
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0030497 | biological_process | fatty acid elongation |
| A | 0047936 | molecular_function | glucose 1-dehydrogenase [NAD(P)+] activity |
| B | 0000166 | molecular_function | nucleotide binding |
| 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 | 0030497 | biological_process | fatty acid elongation |
| B | 0047936 | molecular_function | glucose 1-dehydrogenase [NAD(P)+] activity |
| C | 0000166 | molecular_function | nucleotide binding |
| 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 | 0030497 | biological_process | fatty acid elongation |
| C | 0047936 | molecular_function | glucose 1-dehydrogenase [NAD(P)+] activity |
| D | 0000166 | molecular_function | nucleotide binding |
| 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 | 0030497 | biological_process | fatty acid elongation |
| D | 0047936 | molecular_function | glucose 1-dehydrogenase [NAD(P)+] activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | binding site for residue NAD A 301 |
| Chain | Residue |
| A | GLY12 |
| A | ASN88 |
| A | GLY90 |
| A | VAL111 |
| A | SER139 |
| A | SER140 |
| A | TYR155 |
| A | LYS159 |
| A | PRO185 |
| A | GLY186 |
| A | ILE188 |
| A | SER15 |
| A | HOH407 |
| A | HOH411 |
| A | HOH419 |
| A | HOH458 |
| A | HOH485 |
| A | HOH500 |
| A | HOH505 |
| A | HOH509 |
| A | HOH524 |
| A | GLY18 |
| A | ILE19 |
| A | ASP38 |
| A | LEU39 |
| A | ALA60 |
| A | ASN61 |
| A | VAL62 |
| site_id | AC2 |
| Number of Residues | 27 |
| Details | binding site for residue NAD B 301 |
| Chain | Residue |
| B | GLY12 |
| B | SER15 |
| B | GLY18 |
| B | ILE19 |
| B | ASP38 |
| B | LEU39 |
| B | ALA60 |
| B | ASN61 |
| B | VAL62 |
| B | ASN88 |
| B | GLY90 |
| B | VAL111 |
| B | LEU138 |
| B | SER139 |
| B | SER140 |
| B | TYR155 |
| B | LYS159 |
| B | PRO185 |
| B | GLY186 |
| B | ILE188 |
| B | HOH401 |
| B | HOH412 |
| B | HOH467 |
| B | HOH473 |
| B | HOH483 |
| B | HOH486 |
| B | HOH508 |
| site_id | AC3 |
| Number of Residues | 27 |
| Details | binding site for residue NAD C 301 |
| Chain | Residue |
| C | GLY12 |
| C | SER15 |
| C | GLY18 |
| C | ILE19 |
| C | ASP38 |
| C | LEU39 |
| C | ALA60 |
| C | ASN61 |
| C | VAL62 |
| C | ASN88 |
| C | GLY90 |
| C | VAL111 |
| C | SER139 |
| C | SER140 |
| C | TYR155 |
| C | LYS159 |
| C | PRO185 |
| C | GLY186 |
| C | ILE188 |
| C | THR190 |
| C | HOH410 |
| C | HOH438 |
| C | HOH465 |
| C | HOH471 |
| C | HOH482 |
| C | HOH491 |
| C | HOH522 |
| site_id | AC4 |
| Number of Residues | 26 |
| Details | binding site for residue NAD D 301 |
| Chain | Residue |
| D | GLY186 |
| D | ILE188 |
| D | THR190 |
| D | HOH415 |
| D | HOH433 |
| D | HOH454 |
| D | HOH501 |
| D | HOH511 |
| D | HOH515 |
| D | GLY12 |
| D | SER15 |
| D | GLY18 |
| D | ILE19 |
| D | ASP38 |
| D | LEU39 |
| D | ALA60 |
| D | ASN61 |
| D | VAL62 |
| D | ASN88 |
| D | GLY90 |
| D | VAL111 |
| D | SER139 |
| D | SER140 |
| D | TYR155 |
| D | LYS159 |
| D | PRO185 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SaqrgggifgGphYSAAKAGVlGLAkAMA |
| Chain | Residue | Details |
| A | SER142-ALA170 |
