Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabF, and C16:1-crypto Acyl Carrier Protein, AcpP. Determined by X-ray diffraction at 2.0 Å resolution. Released 6 Oct 2021.
Explore 7L4E in 3D Show helices and sheets RCSB PDB PDBe
7L4E contains 25 α-helices and 28 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 | 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 | 141-150 | 10 | |
| 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 | 215-217 | 3 | |
| β-strand | 223 | 1 | 5 |
| β-strand | 229 | 1 | 4 |
| β-strand | 231 | 1 | 6 |
| 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 | 323-327 | 5 | |
| β-strand | 330-332 | 3 | 1 |
| α-helix | 335-338 | 4 | |
| β-strand | 340 | 1 | 6 |
| α-helix | 342-344 | 3 | |
| α-helix | 345-359 | 15 | |
| β-strand | 361-362 | 2 | 7 |
| β-strand | 365 | 1 | 8 |
| β-strand | 371 | 1 | 5 |
| α-helix | 372 | 1 | |
| β-strand | 378 | 1 | 1 |
| β-strand | 381 | 1 | 8 |
| β-strand | 385-386 | 2 | 7 |
| β-strand | 392-398 | 7 | 1 |
| β-strand | 403-411 | 9 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-15 | 13 | |
| α-helix | 19-21 | 3 | |
| β-strand | 27 | 1 | 9 |
| α-helix | 36-50 | 15 | |
| α-helix | 56-59 | 4 | |
| β-strand | 64 | 1 | 9 |
| α-helix | 65-73 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 3-oxoacyl-[acyl-carrier-protein] synthase 2 | A | protein | 413 | Escherichia coli (strain K12) | P0AAI5 (AlphaFold model) |
| Acyl carrier protein | B | protein | 78 | Escherichia coli (strain K12) | P0A6A8 (AlphaFold model) |
>7L4E_1 3-oxoacyl-[acyl-carrier-protein] synthase 2 (chains A) MSKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCE DIISRKEQRKMDAFIQYGIVAGVQAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHT SLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATACTSGVHNIGHAARIIAY GDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLV LEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGY VNAHGTSTPAGDKAEAQAVKTIFGEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRD QAVPPTINLDNPDEGCDLDFVPHEARQVSGMEYTLCNSFGFGGTNGSLIFKKI
>7L4E_2 Acyl carrier protein (chains B) MSTIEERVKKIIGEQLGVKQEEVTNNASFVEDLGADSLDTVELVMALEEEFDTEIPDEEA EKITTVQAAIDYINGHQA
| ID | Name | Formula | Copies |
|---|---|---|---|
| MU4 | N-[2-(hexadecanoylamino)ethyl]-N~3~-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonoox… | C27 H54 N3 O8 P | 1 |
Water and common crystallization additives (EDO) are not listed.
Structure and Mechanistic Analyses of the Gating Mechanism of Elongating Ketosynthases. Mindrebo, J.T., Chen, A., Kim, W.E. et al. ACS Catal (2021) 11:6787-6799. DOI 10.1021/acscatal.1c00745
Other PDB entries of the same protein (UniProt P0AAI5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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