Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabF, and C16-crypto Acyl Carrier Protein, AcpP. Determined by X-ray diffraction at 2.3 Å resolution. Released 22 Apr 2020.
Explore 6OKG in 3D Show helices and sheets RCSB PDB PDBe
6OKG contains 24 α-helices and 27 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 | 381 | 1 | 8 |
| β-strand | 385-386 | 2 | 7 |
| β-strand | 392-397 | 6 | 1 |
| β-strand | 403-411 | 9 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-15 | 13 | |
| 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) |
>6OKG_1 3-oxoacyl-[acyl-carrier-protein] synthase 2 (chains A) MSKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCE DIISRKEQRKMDAFIQYGIVAGVQAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHT SLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATACTSGVHNIGHAARIIAY GDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLV LEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGY VNAHGTSTPAGDKAEAQAVKTIFGEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRD QAVPPTINLDNPDEGCDLDFVPHEARQVSGMEYTLCNSFGFGGTNGSLIFKKI
>6OKG_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 (NA) are not listed.
Gating mechanism of elongating beta-ketoacyl-ACP synthases. Mindrebo, J.T., Patel, A., Kim, W.E. et al. Nat Commun (2020) 11:1727-1727. DOI 10.1038/s41467-020-15455-x · 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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