The 1.8 a crystal structure and active site architecture of beta-ketoacyl-[acyl carrier protein] synthase III (FABH) from escherichia coli. Determined by X-ray diffraction at 1.8 Å resolution. Released 11 Feb 2000.
Explore 1EBL in 3D Show helices and sheets RCSB PDB PDBe
1EBL contains 36 α-helices and 38 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 | 2-11 | 10 | 1 |
| β-strand | 15-18 | 4 | 2 |
| α-helix | 19-23 | 5 | |
| α-helix | 30-37 | 8 | |
| β-strand | 41-44 | 4 | 2 |
| α-helix | 51-66 | 16 | |
| α-helix | 70-72 | 3 | |
| β-strand | 75-79 | 5 | 1 |
| β-strand | 85-87 | 3 | 3 |
| α-helix | 90-98 | 9 | |
| β-strand | 102 | 1 | 4 |
| β-strand | 105-109 | 5 | 1 |
| α-helix | 111-113 | 3 | |
| α-helix | 114-127 | 14 | |
| β-strand | 133-140 | 8 | 1 |
| α-helix | 142-145 | 4 | |
| α-helix | 151-154 | 4 | |
| β-strand | 157 | 1 | 5 |
| β-strand | 160-169 | 10 | 1 |
| β-strand | 174-181 | 8 | 6 |
| α-helix | 183-188 | 6 | |
| β-strand | 189-190 | 2 | 7 |
| β-strand | 191-192 | 2 | 8 |
| α-helix | 193-194 | 2 | |
| β-strand | 206-207 | 2 | 7 |
| α-helix | 209-230 | 22 | |
| α-helix | 235-237 | 3 | |
| β-strand | 240-243 | 4 | 6 |
| α-helix | 248-258 | 11 | |
| α-helix | 262-264 | 3 | |
| β-strand | 265 | 1 | 6 |
| α-helix | 269-272 | 4 | |
| β-strand | 274 | 1 | 5 |
| α-helix | 276-278 | 3 | |
| α-helix | 279-289 | 11 | |
| β-strand | 298-305 | 8 | 6 |
| β-strand | 309-316 | 8 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-11 | 10 | 1 |
| β-strand | 15-18 | 4 | 9 |
| α-helix | 19-25 | 7 | |
| α-helix | 30-37 | 8 | |
| β-strand | 41-44 | 4 | 9 |
| α-helix | 51-66 | 16 | |
| α-helix | 70-72 | 3 | |
| β-strand | 76-79 | 4 | 1 |
| β-strand | 85-87 | 3 | 8 |
| α-helix | 90-97 | 8 | |
| β-strand | 102 | 1 | 6 |
| β-strand | 105-109 | 5 | 1 |
| α-helix | 111-113 | 3 | |
| α-helix | 114-127 | 14 | |
| β-strand | 133-140 | 8 | 1 |
| α-helix | 142-145 | 4 | |
| α-helix | 151-154 | 4 | |
| β-strand | 157 | 1 | 10 |
| β-strand | 160-169 | 10 | 1 |
| β-strand | 174-181 | 8 | 4 |
| α-helix | 183-188 | 6 | |
| β-strand | 189-190 | 2 | 11 |
| β-strand | 191-192 | 2 | 3 |
| α-helix | 193-194 | 2 | |
| β-strand | 206-207 | 2 | 11 |
| α-helix | 209-230 | 22 | |
| α-helix | 235-237 | 3 | |
| β-strand | 240-243 | 4 | 4 |
| α-helix | 248-257 | 10 | |
| α-helix | 262-264 | 3 | |
| β-strand | 265 | 1 | 4 |
| α-helix | 269-272 | 4 | |
| β-strand | 274 | 1 | 10 |
| α-helix | 276-278 | 3 | |
| α-helix | 279-289 | 11 | |
| β-strand | 298-305 | 8 | 4 |
| β-strand | 309-316 | 8 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Beta-ketoacyl-ACP synthase III | A, B | protein | 317 | Escherichia coli | P0A6R0 (AlphaFold model) |
>1EBL_1 BETA-KETOACYL-ACP SYNTHASE III (chains A, B) MYTKIIGTGSYLPEQVRTNADLEKMVDTSDEWIVTRTGIRERHIAAPNETVSTMGFEAAT RAIEMAGIEKDQIGLIVVATTSATHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALS VADQYVKSGAVKYALVVGSDVLARTCDPTDRGTIIIFGDGAGAAVLAASEEPGIISTHLH ADGSYGELLTLPNADRVNPENSIHLTMAGNEVFKVAVTELAHIVDETLAANNNDRSQLDW LVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKPGQLVL LEAFGGGFTWGSALVRF
| ID | Name | Formula | Copies |
|---|---|---|---|
| COA | Coenzyme a | C21 H36 N7 O16 P3 S | 2 |
The 1.8 A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from escherichia coli. Davies, C., Heath, R.J., White, S.W. et al. Structure (2000) 8:185-195. DOI 10.1016/S0969-2126(00)00094-0 · PubMed
Other PDB entries of the same protein (UniProt P0A6R0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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