Structure of E. coli FabF(C163Q) in complex with Platensimycin. Determined by X-ray diffraction at 2.59 Å resolution. Released 23 May 2006.
Explore 2GFX in 3D Show helices and sheets RCSB PDB PDBe
2GFX contains 20 α-helices and 26 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-13 | 9 | 1 |
| β-strand | 14 | 1 | 2 |
| β-strand | 17 | 1 | 2 |
| α-helix | 20-28 | 9 | |
| β-strand | 34-36 | 3 | 3 |
| β-strand | 49-51 | 3 | 3 |
| α-helix | 64-67 | 4 | |
| α-helix | 72-88 | 17 | |
| α-helix | 97-99 | 3 | |
| β-strand | 100-105 | 6 | 1 |
| α-helix | 111-124 | 14 | |
| α-helix | 126-128 | 3 | |
| α-helix | 133-137 | 5 | |
| α-helix | 141-149 | 9 | |
| β-strand | 156-157 | 2 | 1 |
| α-helix | 162-164 | 3 | |
| α-helix | 165-179 | 15 | |
| β-strand | 184-191 | 8 | 1 |
| α-helix | 196-204 | 9 | |
| β-strand | 208 | 1 | 4 |
| α-helix | 215-218 | 4 | |
| β-strand | 229 | 1 | 4 |
| β-strand | 231 | 1 | 5 |
| β-strand | 232 | 1 | 3 |
| β-strand | 234-242 | 9 | 1 |
| α-helix | 243-247 | 5 | |
| β-strand | 255-264 | 10 | 1 |
| β-strand | 268 | 1 | 6 |
| β-strand | 271 | 1 | 6 |
| α-helix | 277-290 | 14 | |
| α-helix | 294-296 | 3 | |
| β-strand | 297-301 | 5 | 1 |
| α-helix | 308-322 | 15 | |
| α-helix | 325-327 | 3 | |
| β-strand | 330-332 | 3 | 1 |
| α-helix | 335-338 | 4 | |
| β-strand | 340 | 1 | 5 |
| α-helix | 342-344 | 3 | |
| α-helix | 345-358 | 14 | |
| β-strand | 361-362 | 2 | 7 |
| β-strand | 365 | 1 | 8 |
| β-strand | 378 | 1 | 1 |
| β-strand | 381 | 1 | 8 |
| β-strand | 385-386 | 2 | 7 |
| β-strand | 392-399 | 8 | 1 |
| β-strand | 403-411 | 9 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 3-oxoacyl-[acyl-carrier-protein] synthase 2 | A | protein | 427 | Escherichia coli | P0AAI5 (AlphaFold model) |
>2GFX_1 3-oxoacyl-[acyl-carrier-protein] synthase 2 (chains A) MRGSHHHHHHGSACVSKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAY ATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAGVQAMQDSGLEITEENATRIGAAIG SGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATAQTS GVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKE RDGFVLGDGAGMLVLEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMAN ALRDAGIEASQIGYVNAHGTSTPAGDKAEAQAVKTIFGEAASRVLVSSTKSMTGHLLGAA GAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSGMEYTLCNSFGFGGTNG SLIFKKI
| ID | Name | Formula | Copies |
|---|---|---|---|
| PMN | Platensimycin | C24 H27 N O7 | 1 |
Platensimycin is a selective FabF inhibitor with potent antibiotic properties. Wang, J., Soisson, S.M., Young, K. et al. Nature (2006) 441:358-361. DOI 10.1038/nature04784 · PubMed
Other PDB entries of the same protein (UniProt P0AAI5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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