Crosslinked Crystal Structure of Malonyl-CoA Acyl Carrier Protein Transacylase, FabD, and Acyl Carrier Protein, AcpP. Determined by X-ray diffraction at 1.9 Å resolution. Released 22 Jul 2020.
Explore 6U0J in 3D Show helices and sheets RCSB PDB PDBe
6U0J contains 21 α-helices and 13 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 | 4-8 | 5 | 1 |
| α-helix | 20-25 | 6 | |
| α-helix | 27-40 | 14 | |
| α-helix | 44-50 | 7 | |
| α-helix | 53-56 | 4 | |
| α-helix | 59-79 | 21 | |
| α-helix | 82-85 | 4 | |
| β-strand | 87-90 | 4 | 1 |
| α-helix | 94-101 | 8 | |
| α-helix | 107-124 | 18 | |
| β-strand | 130-136 | 7 | 2 |
| α-helix | 140-150 | 11 | |
| β-strand | 156-163 | 8 | 2 |
| β-strand | 166-172 | 7 | 2 |
| α-helix | 173-185 | 13 | |
| β-strand | 190-193 | 4 | 2 |
| α-helix | 203-205 | 3 | |
| α-helix | 206-217 | 12 | |
| β-strand | 228-229 | 2 | 1 |
| β-strand | 236 | 1 | 1 |
| α-helix | 240-250 | 11 | |
| β-strand | 255-256 | 2 | 2 |
| α-helix | 257-266 | 10 | |
| β-strand | 271-274 | 4 | 1 |
| α-helix | 280-288 | 9 | |
| β-strand | 293-296 | 4 | 1 |
| α-helix | 300-307 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-15 | 13 | |
| α-helix | 19-21 | 3 | |
| β-strand | 27 | 1 | 3 |
| α-helix | 36-50 | 15 | |
| α-helix | 56-59 | 4 | |
| β-strand | 64 | 1 | 3 |
| α-helix | 65-72 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Malonyl CoA-acyl carrier protein transacylase | A | protein | 312 | Escherichia coli (strain K12) | P0AAI9 (AlphaFold model) |
| Acyl carrier protein | B | protein | 85 | Escherichia coli (strain K12 / DH10B) | P0A6A8 (AlphaFold model) |
>6U0J_1 Malonyl CoA-acyl carrier protein transacylase (chains A) GSHMTQFAFVFPGQGSQTVGMLADMAASYPIVEETFAEASAALGYDLWALTQQGPAEELN KTWQTQPALLTASVALYRVWQQQGGKAPAMMAGHCLGEYSALVCAGVIDFADAVRLVEMR GKFMQEAVPEGTGAMAAIIGLDDASIAKACEEAAEGQVVSPVNFNSPGQVVIAGHKEAVE RAGAACKAAGAKRALPLPVSVPSHCALMKPAADKLAVELAKITFNAPTVPVVNNVDVKCE TNGDAIRDALVRQLYNPVQWTKSVEYMAAQGVEHLYEVGPGKVLTGLTKRIVDTLTASAL NEPSAMAAALEL
>6U0J_2 Acyl carrier protein (chains B) MSTIEERVKKIIGEQLGVKQEEVTNNASFVEDLGADSLDTVELVMALEEEFDTEIPDEEA EKITTVQAAIDYINGHQASHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| 9EF | N-[2-(acetylamino)ethyl]-N~3~-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)buta… | C13 H26 N3 O8 P | 1 |
Water and common crystallization additives (SO4, EDO) are not listed.
Interfacial plasticity facilitates high reaction rate of E. coli FAS malonyl-CoA:ACP transacylase, FabD. Misson, L.E., Mindrebo, J.T., Davis, T.D. et al. Proc Natl Acad Sci U S A (2020) 117:24224-24233. DOI 10.1073/pnas.2009805117 · PubMed
Other PDB entries of the same protein (UniProt P0AAI9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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