Crystal structure of the periplasmic domain of IgaA from Escherichia coli. Determined by X-ray diffraction at 1.8 Å resolution. Released 17 Jul 2024.
Explore 9BIY in 3D Show helices and sheets RCSB PDB PDBe
9BIY contains 15 α-helices and 14 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 | 376-379 | 4 | 1 |
| α-helix | 382-386 | 5 | |
| β-strand | 395-405 | 11 | 1 |
| β-strand | 424-430 | 7 | 1 |
| α-helix | 437-439 | 3 | |
| α-helix | 442-458 | 17 | |
| α-helix | 470-479 | 10 | |
| β-strand | 482-484 | 3 | 2 |
| α-helix | 487-497 | 11 | |
| α-helix | 505-514 | 10 | |
| α-helix | 520-529 | 10 | |
| β-strand | 536 | 1 | 3 |
| β-strand | 537-539 | 3 | 2 |
| α-helix | 541-569 | 29 | |
| α-helix | 573-574 | 2 | |
| β-strand | 578-582 | 5 | 1 |
| α-helix | 592-594 | 3 | |
| α-helix | 598-600 | 3 | |
| α-helix | 603-617 | 15 | |
| β-strand | 620-633 | 14 | 1 |
| β-strand | 639-644 | 6 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 50-52 | 3 | 3 |
| α-helix | 55-58 | 4 | |
| β-strand | 63-75 | 13 | 3 |
| α-helix | 81-83 | 3 | |
| α-helix | 85-98 | 14 | |
| β-strand | 103-108 | 6 | 3 |
| β-strand | 111-112 | 2 | 3 |
| β-strand | 120-131 | 12 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Intracellular growth attenuator protein igaA | A | protein | 275 | Escherichia coli | P45800 (AlphaFold model) |
| Outer membrane lipoprotein RcsF | B | protein | 88 | Escherichia coli | P69411 (AlphaFold model) |
>9BIY_1 Intracellular growth attenuator protein igaA (chains A) SAQTIEATSVKQLADAGVRVGDTLRISGTGMCNIRTSGTWSAKTNSPFLPFDCSQIIWND ARSLPLPESELVNKATALTEAVNRQLHPKPEDESRVSASLRSAIQKSGMVLLDDFGDIVL KTADLCSAKDDCVRLKNALVNLGNSKDWDALVKRANAGKLDGVNVLLRPVSAESLDNLVA TSTAPFITHETARAAQSLNSPAPGGFLIVSDEGSDFVDQPWPSASLYDYPPQEQWNAFQK LAQMLMHTPFNAEGIVTKIFTDANGTQHIGLHPIP
>9BIY_2 Outer membrane lipoprotein RcsF (chains B) RATPVRIYTNAEELVGKPFRDLGEVSGDSCQASNQDSPPSIPTARKRMQINASKMKANAV LLHSCEVTSGTPGCYRQAVCIGSALNIT
Molecular insights into the initiation step of the Rcs signaling pathway. Watanabe, N., Savchenko, A. Structure (2024) 32:1381-1393.e4. DOI 10.1016/j.str.2024.06.003 · PubMed
Other PDB entries of the same protein (UniProt P45800 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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