Crystal structure of InlA G194S+S Y369S/hEC1 complex. Determined by X-ray diffraction at 1.8 Å resolution. Released 28 Aug 2007.
Explore 2OMU in 3D Show helices and sheets RCSB PDB PDBe
2OMU contains 23 α-helices and 42 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 | 42-43 | 2 | 1 |
| α-helix | 44-47 | 4 | |
| α-helix | 51-60 | 10 | |
| β-strand | 69-70 | 2 | 1 |
| α-helix | 72-75 | 4 | |
| β-strand | 80-82 | 3 | 2 |
| α-helix | 94-96 | 3 | |
| β-strand | 102-104 | 3 | 2 |
| α-helix | 114-116 | 3 | |
| β-strand | 124-126 | 3 | 2 |
| α-helix | 136-138 | 3 | |
| β-strand | 146-148 | 3 | 2 |
| α-helix | 158-160 | 3 | |
| β-strand | 168-170 | 3 | 2 |
| α-helix | 180-182 | 3 | |
| β-strand | 190-192 | 3 | 2 |
| α-helix | 202-204 | 3 | |
| β-strand | 212-214 | 3 | 2 |
| α-helix | 224-228 | 5 | |
| β-strand | 234-236 | 3 | 2 |
| α-helix | 246-250 | 5 | |
| β-strand | 256-258 | 3 | 2 |
| α-helix | 268-272 | 5 | |
| β-strand | 278-280 | 3 | 2 |
| α-helix | 290-292 | 3 | |
| β-strand | 300-302 | 3 | 2 |
| α-helix | 312-314 | 3 | |
| β-strand | 322-324 | 3 | 2 |
| α-helix | 334-338 | 5 | |
| β-strand | 344-346 | 3 | 2 |
| α-helix | 356-358 | 3 | |
| β-strand | 366-368 | 3 | 2 |
| α-helix | 378-382 | 5 | |
| β-strand | 388-390 | 3 | 2 |
| β-strand | 398 | 1 | 3 |
| α-helix | 400-402 | 3 | |
| β-strand | 410-412 | 3 | 2 |
| β-strand | 416-419 | 4 | 4 |
| α-helix | 420-422 | 3 | |
| β-strand | 423-424 | 2 | 5 |
| β-strand | 428-432 | 5 | 6 |
| β-strand | 436 | 1 | 3 |
| α-helix | 441 | 1 | |
| β-strand | 442 | 1 | 3 |
| α-helix | 443-445 | 3 | |
| β-strand | 447-448 | 2 | 4 |
| α-helix | 449-451 | 3 | |
| β-strand | 453-455 | 3 | 6 |
| β-strand | 458-462 | 5 | 6 |
| β-strand | 469-480 | 12 | 4 |
| β-strand | 483-494 | 12 | 4 |
| β-strand | 495-496 | 2 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-3 | 2 | 7 |
| β-strand | 7-10 | 4 | 8 |
| β-strand | 19-23 | 5 | 9 |
| β-strand | 25-26 | 2 | 7 |
| α-helix | 27-30 | 4 | |
| β-strand | 35-39 | 5 | 8 |
| β-strand | 41 | 1 | 10 |
| β-strand | 45 | 1 | 10 |
| β-strand | 51-53 | 3 | 9 |
| β-strand | 59-62 | 4 | 9 |
| β-strand | 73-81 | 9 | 8 |
| β-strand | 87 | 1 | 8 |
| β-strand | 92-99 | 8 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Internalin-A | A | protein | 462 | Listeria monocytogenes | P0DJM0 (AlphaFold model) |
| Epithelial-cadherin | B | protein | 105 | Homo sapiens | P12830 (AlphaFold model) |
>2OMU_1 Internalin-A (chains A) ATITQDTPINQIFTDTALAEKMKTVLGKTNVTDTVSQTDLDQVTTLQADRLGIKSIDGVE YLNNLTQINFSNNQLTDITPLKNLTKLVDILMNNNQIADITPLANLTNLTGLTLFNNQIT DIDPLKNLTNLNRLELSSNTISDISALSGLTSLQQLSFSSNQVTDLKPLANLTTLERLDI SSNKVSDISVLAKLTNLESLIATNNQISDITPLGILTNLDELSLNGNQLKDIGTLASLTN LTDLDLANNQISNLAPLSGLTKLTELKLGANQISNISPLAGLTALTNLELNENQLEDISP ISNLKNLTYLTLYFNNISDISPVSSLTKLQRLFFSNNKVSDVSSLANLTNINWLSAGHNQ ISDLTPLANLTRITQLGLNDQAWTNAPVNYKANVSIPNTVKNVTGALIAPATISDGGSYT EPDITWNLPSYTNEVSYTFSQPVTIGKGTTTFSGTVTQPLKA
>2OMU_2 Epithelial-cadherin (chains B) GPLGSWVIPPISCPENEKGPFPKNLVQIKSNKDKEGKVFYSITGQGADTPPVGVFIIERE TGWLKVTEPLDRERIATYTLFSHAVSSNGNAVEDPMEILITVTDQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 1 |
Water and common crystallization additives (CL) are not listed.
Thermodynamically reengineering the listerial invasion complex InlA/E-cadherin. Wollert, T., Heinz, D.W., Schubert, W.D. Proc Natl Acad Sci U S A (2007) 104:13960-13965. DOI 10.1073/pnas.0702199104 · PubMed
Other PDB entries of the same protein (UniProt P0DJM0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2OMU directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.