Structure of mitochondrial beta-ketoacyl synthase. Determined by X-ray diffraction at 1.8 Å resolution. Released 13 Dec 2005.
Explore 2C9H in 3D Show helices and sheets RCSB PDB PDBe
2C9H contains 24 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 | 29-38 | 10 | 1 |
| β-strand | 41-42 | 2 | 1 |
| α-helix | 44-52 | 9 | |
| β-strand | 58-60 | 3 | 2 |
| α-helix | 64-66 | 3 | |
| β-strand | 73-75 | 3 | 2 |
| α-helix | 76-78 | 3 | |
| β-strand | 79 | 1 | 3 |
| β-strand | 86 | 1 | 3 |
| α-helix | 88-90 | 3 | |
| α-helix | 96-99 | 4 | |
| α-helix | 102-118 | 17 | |
| α-helix | 125-129 | 5 | |
| β-strand | 131-137 | 7 | 1 |
| α-helix | 142-155 | 14 | |
| α-helix | 157-159 | 3 | |
| α-helix | 164-168 | 5 | |
| α-helix | 172-181 | 10 | |
| β-strand | 187-188 | 2 | 1 |
| α-helix | 193-195 | 3 | |
| α-helix | 196-210 | 15 | |
| β-strand | 215-222 | 8 | 1 |
| α-helix | 227-235 | 9 | |
| β-strand | 239 | 1 | 4 |
| β-strand | 259 | 1 | 4 |
| β-strand | 261 | 1 | 5 |
| β-strand | 262 | 1 | 2 |
| β-strand | 264-272 | 9 | 1 |
| α-helix | 273-279 | 7 | |
| β-strand | 285-294 | 10 | 1 |
| α-helix | 302-303 | 2 | |
| α-helix | 307-320 | 14 | |
| α-helix | 324-326 | 3 | |
| β-strand | 327-331 | 5 | 1 |
| α-helix | 338-352 | 15 | |
| α-helix | 353-357 | 5 | |
| β-strand | 360-362 | 3 | 1 |
| α-helix | 365-368 | 4 | |
| β-strand | 370 | 1 | 5 |
| α-helix | 372-374 | 3 | |
| α-helix | 375-389 | 15 | |
| β-strand | 391-392 | 2 | 6 |
| α-helix | 393-394 | 2 | |
| β-strand | 395 | 1 | 7 |
| β-strand | 411 | 1 | 7 |
| β-strand | 415-416 | 2 | 6 |
| β-strand | 424-431 | 8 | 1 |
| β-strand | 435-442 | 8 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mitochondrial beta-ketoacyl synthase | A | protein | 444 | HOMO SAPIENS | Q9NWU1 (AlphaFold model) |
>2C9H_1 MITOCHONDRIAL BETA-KETOACYL SYNTHASE (chains A) MHHHHHHSSGVDLGTENLYFQSMRLHRRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVS LVGEEYKSIPCSVAAYVPRGSDEGQFNEQNFVSKSDIKSMSSPTIMAIGAAELAMKDSGW HPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIR YKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALS TNSDPKLACRPFHPKRDGFVMGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHIT APDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAENKAIKHLFKDHAYALA VSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTE KRFIGLTNSFGFGGTNATLCIAGL
| ID | Name | Formula | Copies |
|---|---|---|---|
| NI | Nickel (II) ion | Ni | 1 |
Structure of Mitochondrial Beta-Ketoacyl Synthase. Bunkoczi, G., Wu, X., Smee, C. et al. To be published.
Other PDB entries of the same protein (UniProt Q9NWU1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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