Structure of E.coli FabD complexed with sulfate. Determined by X-ray diffraction at 1.76 Å resolution. Released 30 May 2006.
Explore 2G2O in 3D Show helices and sheets RCSB PDB PDBe
2G2O contains 17 α-helices and 10 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 | 4-8 | 5 | 1 |
| α-helix | 20-25 | 6 | |
| α-helix | 28-40 | 13 | |
| 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 | 93-101 | 9 | |
| α-helix | 107-123 | 17 | |
| β-strand | 130-136 | 7 | 2 |
| α-helix | 140-151 | 12 | |
| β-strand | 156-163 | 8 | 2 |
| β-strand | 166-172 | 7 | 2 |
| α-helix | 173-186 | 14 | |
| β-strand | 190-193 | 4 | 2 |
| α-helix | 203-205 | 3 | |
| α-helix | 206-217 | 12 | |
| α-helix | 222-224 | 3 | |
| β-strand | 228 | 1 | 1 |
| α-helix | 240-252 | 13 | |
| 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 | 300-308 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Malonyl CoA-acyl carrier protein transacylase | A | protein | 308 | Escherichia coli | P0AAI9 (AlphaFold model) |
>2G2O_1 Malonyl CoA-acyl carrier protein transacylase (chains A) TQFAFVFPGQGSQTVGMLADMAASYPIVEETFAEASAALGYDLWALTQQGPAEELNKTWQ TQPALLTASVALYRVWQQQGGKAPAMMAGHSLGEYSALVCAGVIDFADAVRLVEMRGKFM QEAVPEGTGAMAAIIGLDDASIAKACEEAAEGQVVSPVNFNSPGQVVIAGHKEAVERAGA ACKAAGAKRALPLPVSVPSHCALMKPAADKLAVELAKITFNAPTVPVVNNVDVKCETNGD AIRDALVRQLYNPVQWTKSVEYMAAQGVEHLYEVGPGKVLTGLTKRIVDTLTASALNEPS AMAAALEL
Mapping the active site of Escherichia coli malonyl-CoA-acyl carrier protein transacylase (FabD) by protein crystallography. Oefner, C., Schulz, H., D'Arcy, A. et al. Acta Crystallogr D Biol Crystallogr (2006) 62:613-618. DOI 10.1107/S0907444906009474 · 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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