3RSH
Structure of 3-ketoacyl-(acyl-carrier-protein)reductase (FabG) from Vibrio cholerae O1 complexed with NADP+ (space group P62)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004316 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| 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 | 0030497 | biological_process | fatty acid elongation |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| B | 0004316 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006631 | biological_process | fatty acid metabolic process |
| 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 | 0030497 | biological_process | fatty acid elongation |
| B | 0050661 | molecular_function | NADP binding |
| B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 249 |
| Chain | Residue |
| A | ARG133 |
| A | ARG176 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 250 |
| Chain | Residue |
| A | ARG19 |
| A | GLY20 |
| A | LYS23 |
| A | LYS23 |
| A | HOH277 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 251 |
| Chain | Residue |
| A | LYS123 |
| A | LYS103 |
| A | GLU104 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 252 |
| Chain | Residue |
| A | ILE93 |
| A | ARG95 |
| A | HOH321 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 253 |
| Chain | Residue |
| A | GLY83 |
| A | GLY83 |
| A | LYS132 |
| A | LYS132 |
| site_id | AC6 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAP A 254 |
| Chain | Residue |
| A | GLY16 |
| A | ALA17 |
| A | SER18 |
| A | ARG19 |
| A | ILE21 |
| A | THR41 |
| A | LEU62 |
| A | ASN63 |
| A | VAL64 |
| A | ASN90 |
| A | ALA91 |
| A | GLY92 |
| A | VAL140 |
| A | GLY141 |
| A | SER142 |
| A | TYR155 |
| A | LYS159 |
| A | PRO185 |
| A | GLY186 |
| A | ILE188 |
| A | THR190 |
| A | MET192 |
| A | THR193 |
| A | HOH298 |
| A | HOH306 |
| A | HOH309 |
| A | HOH320 |
| A | HOH322 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 255 |
| Chain | Residue |
| A | ILE248 |
| A | ILE248 |
| B | LYS167 |
| B | LYS167 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 249 |
| Chain | Residue |
| B | ARG19 |
| B | GLY20 |
| B | LYS23 |
| B | LYS23 |
| B | HOH278 |
| B | HOH297 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 250 |
| Chain | Residue |
| B | LYS103 |
| B | GLU104 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 251 |
| Chain | Residue |
| A | SER2 |
| A | ARG32 |
| B | MET1 |
| B | SER2 |
| B | ARG32 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 252 |
| Chain | Residue |
| B | ILE93 |
| B | ARG95 |
| B | HOH269 |
| B | HOH309 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 253 |
| Chain | Residue |
| B | ARG133 |
| B | ARG176 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 254 |
| Chain | Residue |
| B | GLY83 |
| B | GLY83 |
| B | LYS132 |
| B | LYS132 |
| site_id | BC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAP B 255 |
| Chain | Residue |
| B | GLY16 |
| B | SER18 |
| B | ARG19 |
| B | ILE21 |
| B | THR41 |
| B | LEU62 |
| B | ASN63 |
| B | VAL64 |
| B | ASN90 |
| B | ALA91 |
| B | ILE93 |
| B | VAL140 |
| B | GLY141 |
| B | TYR155 |
| B | LYS159 |
| B | PRO185 |
| B | GLY186 |
| B | ILE188 |
| B | THR190 |
| B | HOH286 |
| B | HOH288 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 261 |
| Chain | Residue |
| A | LYS167 |
| A | LYS167 |
| B | ILE248 |
| B | ILE248 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SvvgtmgnagQanYAAAKAGViGFTkSMA |
| Chain | Residue | Details |
| A | SER142-ALA170 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10001","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
