4I08
Crystal structure of beta-ketoacyl-acyl carrier protein reductase (FabG) from Vibrio cholerae in complex with NADPH
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 | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 301 |
Chain | Residue |
A | SER2 |
A | ARG32 |
B | SER2 |
B | PHE4 |
B | ARG32 |
site_id | AC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 A 302 |
Chain | Residue |
A | ARG133 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 303 |
Chain | Residue |
A | HOH448 |
A | ASP96 |
A | ASN97 |
A | GLY151 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 A 304 |
Chain | Residue |
A | ARG101 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 305 |
Chain | Residue |
A | GLY92 |
A | ILE93 |
A | THR94 |
A | NDP306 |
site_id | AC6 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NDP A 306 |
Chain | Residue |
A | GLY16 |
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 | EDO305 |
A | HOH402 |
A | HOH442 |
A | HOH461 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 301 |
Chain | Residue |
B | ARG133 |
B | ARG176 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 302 |
Chain | Residue |
B | ILE93 |
B | ARG95 |
B | HOH445 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 303 |
Chain | Residue |
B | GLY82 |
B | GLY83 |
B | LYS132 |
B | EDO307 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 304 |
Chain | Residue |
B | ARG19 |
B | GLY20 |
B | LYS23 |
B | LYS23 |
B | HOH456 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 305 |
Chain | Residue |
B | ALA150 |
B | ARG171 |
B | GLU172 |
B | ARG176 |
B | HOH446 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 306 |
Chain | Residue |
B | LYS103 |
B | GLU104 |
B | HOH409 |
B | HOH452 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B 307 |
Chain | Residue |
B | GLY83 |
B | VAL84 |
B | VAL125 |
B | GLY128 |
B | MET129 |
B | LYS132 |
B | SO4303 |
site_id | BC5 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE NDP B 308 |
Chain | Residue |
B | GLY16 |
B | ALA17 |
B | SER18 |
B | ARG19 |
B | ILE21 |
B | THR41 |
B | LEU62 |
B | ASN63 |
B | VAL64 |
B | ASN90 |
B | ALA91 |
B | VAL140 |
B | GLY141 |
B | TYR155 |
B | LYS159 |
B | PRO185 |
B | GLY186 |
B | ILE188 |
B | THR190 |
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 |