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 | 0004316 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity |
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 | 0004316 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity |
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 | 0004316 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity |
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 | 0004316 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity |
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 |