Beta-ketoacyl carrier protein synthase as a drug target, implications from the crystal structure of a complex with the inhibitor cerulenin. Determined by X-ray diffraction at 2.65 Å resolution. Released 6 Apr 1999.
Explore 1B3N in 3D Show helices and sheets RCSB PDB PDBe
1B3N contains 20 α-helices and 24 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 | 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 | 243-249 | 7 | |
| β-strand | 255-264 | 10 | 1 |
| α-helix | 271-273 | 3 | |
| 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 | 334-336 | 3 | |
| β-strand | 340 | 1 | 6 |
| α-helix | 342-344 | 3 | |
| α-helix | 345-359 | 15 | |
| β-strand | 361-362 | 2 | 7 |
| β-strand | 371 | 1 | 5 |
| β-strand | 378 | 1 | 1 |
| β-strand | 385-386 | 2 | 7 |
| β-strand | 392-399 | 8 | 1 |
| β-strand | 403-410 | 8 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (ketoacyl acyl carrier protein synthase 2) | A | protein | 412 | Escherichia coli | P0AAI5 (AlphaFold model) |
>1B3N_1 PROTEIN (KETOACYL ACYL CARRIER PROTEIN SYNTHASE 2) (chains A) SKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCED IISRKEQRKMDAFIQYGIVAGVQAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTS LMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATACTSGVHNIGHAARIIAYG DADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLVL EEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYV NAHGTSTPAGDKAEAQAVKTIFGEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQ AVPPTINLDNPDEGCDLDFVPHEARQVSGMEYTLCNSFGFGGTNGSLIFKKI
| ID | Name | Formula | Copies |
|---|---|---|---|
| CER | (2S, 3R)-3-hydroxy-4-oxo-7,10-trans,trans-dodecadienamide | C12 H19 N O3 | 1 |
Structure of the complex between the antibiotic cerulenin and its target, beta-ketoacyl-acyl carrier protein synthase. Moche, M., Schneider, G., Edwards, P. et al. J Biol Chem (1999) 274:6031-6034. DOI 10.1074/jbc.274.10.6031 · 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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