E. coli FabF mutant -C163Q. Determined by X-ray diffraction at 2.7 Å resolution. Released 28 Jan 2026.
Explore 9LPL in 3D Show helices and sheets RCSB PDB PDBe
9LPL contains 46 α-helices and 52 β-strands across 2 chains. 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 | 52-53 | 2 | |
| 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 | 141-150 | 10 | |
| β-strand | 156-157 | 2 | 1 |
| β-strand | 159 | 1 | 4 |
| α-helix | 162-164 | 3 | |
| α-helix | 165-178 | 14 | |
| β-strand | 184-191 | 8 | 1 |
| α-helix | 196-204 | 9 | |
| β-strand | 208 | 1 | 5 |
| β-strand | 223 | 1 | 6 |
| β-strand | 229 | 1 | 5 |
| β-strand | 231 | 1 | 7 |
| β-strand | 232 | 1 | 3 |
| β-strand | 234-242 | 9 | 1 |
| α-helix | 243-248 | 6 | |
| β-strand | 255-264 | 10 | 1 |
| α-helix | 277-290 | 14 | |
| α-helix | 294-296 | 3 | |
| β-strand | 297-301 | 5 | 1 |
| α-helix | 308-322 | 15 | |
| α-helix | 323-326 | 4 | |
| β-strand | 330-332 | 3 | 1 |
| α-helix | 335-338 | 4 | |
| β-strand | 340 | 1 | 7 |
| α-helix | 342-344 | 3 | |
| α-helix | 345-359 | 15 | |
| β-strand | 361-362 | 2 | 8 |
| β-strand | 365 | 1 | 9 |
| β-strand | 371 | 1 | 6 |
| α-helix | 372 | 1 | |
| β-strand | 378 | 1 | 1 |
| β-strand | 381 | 1 | 9 |
| β-strand | 385-386 | 2 | 8 |
| β-strand | 392-399 | 8 | 1 |
| α-helix | 400-402 | 3 | |
| β-strand | 403-410 | 8 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-13 | 9 | 10 |
| α-helix | 20-28 | 9 | |
| β-strand | 34-36 | 3 | 11 |
| β-strand | 49-51 | 3 | 11 |
| α-helix | 52-54 | 3 | |
| α-helix | 64-67 | 4 | |
| α-helix | 72-88 | 17 | |
| α-helix | 90-92 | 3 | |
| α-helix | 97-99 | 3 | |
| β-strand | 100-105 | 6 | 10 |
| α-helix | 111-124 | 14 | |
| α-helix | 126-128 | 3 | |
| α-helix | 133-137 | 5 | |
| α-helix | 141-150 | 10 | |
| β-strand | 156-157 | 2 | 10 |
| β-strand | 159 | 1 | 4 |
| α-helix | 162-164 | 3 | |
| α-helix | 165-179 | 15 | |
| β-strand | 184-191 | 8 | 10 |
| α-helix | 196-204 | 9 | |
| β-strand | 208 | 1 | 12 |
| α-helix | 215-217 | 3 | |
| β-strand | 223 | 1 | 13 |
| β-strand | 229 | 1 | 12 |
| β-strand | 231 | 1 | 14 |
| β-strand | 232 | 1 | 11 |
| β-strand | 234-242 | 9 | 10 |
| α-helix | 243-248 | 6 | |
| β-strand | 255-264 | 10 | 10 |
| α-helix | 277-290 | 14 | |
| α-helix | 294-296 | 3 | |
| β-strand | 297-301 | 5 | 10 |
| α-helix | 308-322 | 15 | |
| α-helix | 323-326 | 4 | |
| β-strand | 330-332 | 3 | 10 |
| α-helix | 335-338 | 4 | |
| β-strand | 340 | 1 | 14 |
| α-helix | 342-344 | 3 | |
| α-helix | 345-359 | 15 | |
| β-strand | 361-362 | 2 | 15 |
| β-strand | 365 | 1 | 16 |
| β-strand | 371 | 1 | 13 |
| α-helix | 372 | 1 | |
| β-strand | 378 | 1 | 10 |
| β-strand | 381 | 1 | 16 |
| β-strand | 385-386 | 2 | 15 |
| β-strand | 392-399 | 8 | 10 |
| α-helix | 400-402 | 3 | |
| β-strand | 403-410 | 8 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 3-oxoacyl-[acyl-carrier-protein] synthase 2 | A, B | protein | 443 | Escherichia coli K-12 | P0AAI5 (AlphaFold model) |
>9LPL_1 3-oxoacyl-[acyl-carrier-protein] synthase 2 (chains A, B) HHHHHHSSGLVPRGSHMVSKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDT SAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAGVQAMQDSGLEITEENATRIGA AIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATA QTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPW DKERDGFVLGDGAGMLVLEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALA MANALRDAGIEASQIGYVNAHGTSTPAGDKAEAQAVKTIFGEAASRVLVSSTKSMTGHLL GAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSGMEYTLCNSFGFGG TNGSLIFKKIKLAAALEHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1EWE | 3-(3-((2S,3S,5S,5aR,6S,12cR)-11-(tert-butyl)-2,6-dimethyl-7-oxo-1,2,3,4,5,5a,6,… | C34 H37 N O7 S | 2 |
Structure of E. coli FabF(C163Q) in complex with Platensimycin analog. Chen, L., Huang, Y. To be published.
Other PDB entries of the same protein (UniProt P0AAI5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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