Crystal structure of Acinetobacter baumannii DsbA in complex with EF-Tu. Determined by X-ray diffraction at 2.15 Å resolution. Released 18 Jun 2014.
Explore 4P3Y in 3D Show helices and sheets RCSB PDB PDBe
4P3Y contains 25 α-helices and 35 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 |
|---|---|---|---|
| α-helix | 10-11 | 2 | |
| β-strand | 12-18 | 7 | 1 |
| α-helix | 25-40 | 16 | |
| α-helix | 42-47 | 6 | |
| β-strand | 66-71 | 6 | 1 |
| β-strand | 76-81 | 6 | 1 |
| α-helix | 85-94 | 10 | |
| β-strand | 101-107 | 7 | 1 |
| α-helix | 114-126 | 13 | |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 138-140 | 3 | |
| α-helix | 144-160 | 17 | |
| α-helix | 165-167 | 3 | |
| β-strand | 170-172 | 3 | 1 |
| α-helix | 175-179 | 5 | |
| α-helix | 183-199 | 17 | |
| α-helix | 201-205 | 5 | |
| α-helix | 206-208 | 3 | |
| α-helix | 210-211 | 2 | |
| β-strand | 212-214 | 3 | 2 |
| β-strand | 217-221 | 5 | 3 |
| β-strand | 225-231 | 7 | 3 |
| β-strand | 234 | 1 | 2 |
| β-strand | 236-238 | 3 | 4 |
| β-strand | 242-246 | 5 | 2 |
| β-strand | 252-255 | 4 | 2 |
| β-strand | 256-261 | 6 | 3 |
| β-strand | 264-266 | 3 | 3 |
| β-strand | 268-270 | 3 | 4 |
| β-strand | 274-279 | 6 | 3 |
| α-helix | 284-286 | 3 | |
| β-strand | 289 | 1 | 5 |
| β-strand | 291 | 1 | 5 |
| β-strand | 292-294 | 3 | 2 |
| β-strand | 301-311 | 11 | 6 |
| α-helix | 312-313 | 2 | |
| α-helix | 314-316 | 3 | |
| β-strand | 323-324 | 2 | 7 |
| β-strand | 330-333 | 4 | 6 |
| β-strand | 336-343 | 8 | 6 |
| α-helix | 344-345 | 2 | |
| β-strand | 350-351 | 2 | 7 |
| β-strand | 356-368 | 13 | 6 |
| β-strand | 374-379 | 6 | 6 |
| β-strand | 382-392 | 11 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5 | 1 | 8 |
| β-strand | 9 | 1 | 8 |
| β-strand | 10-11 | 2 | 9 |
| β-strand | 24-29 | 6 | 9 |
| α-helix | 35-48 | 14 | |
| β-strand | 55-59 | 5 | 9 |
| α-helix | 66-80 | 15 | |
| α-helix | 84-96 | 13 | |
| α-helix | 105-112 | 8 | |
| α-helix | 113-115 | 3 | |
| α-helix | 119-126 | 8 | |
| α-helix | 129-144 | 16 | |
| β-strand | 152-155 | 4 | 9 |
| β-strand | 159-161 | 3 | 9 |
| α-helix | 166-179 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Elongation factor Tu 1 | A | protein | 394 | Escherichia coli BL21(DE3) | P0CE47 (AlphaFold model) |
| Thiol:disulfide interchange protein | B | protein | 182 | Acinetobacter baumannii AYE | A0A0D5YNX0 (AlphaFold model) |
>4P3Y_1 Elongation factor Tu 1 (chains A) MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARG ITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHI LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALE GDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVG EEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIK PHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMV VTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLG
>4P3Y_2 Thiol:disulfide interchange protein (chains B) SNAAGKDYTVIANPGKVEVPGKIEVREFFWYGCPHCFKLEPHMQTWLKQIPSDVRFVRTP AAMNKVWEQGARTYYTSEALGVRKRTHLPLFHAIQVNGQQIFDQASAAKFFTRYGVPEQK FNSTYNSFAVTAKVAESNKLAQQYQLTGVPAVVVNGKYVVQGEDGKVTQVLNYLIEKERK AK
Water and common crystallization additives (GOL) are not listed.
Structure of the Acinetobacter baumannii Dithiol Oxidase DsbA Bound to Elongation Factor EF-Tu Reveals a Novel Protein Interaction Site. Premkumar, L., Kurth, F., Duprez, W. et al. J Biol Chem (2014) 289:19869-19880. DOI 10.1074/jbc.M114.571737 · PubMed
Other PDB entries of the same protein (UniProt P0CE47 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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