9BJ0: Periplasmic domain of IgaA from Escherichia coli

Crystal structure of the periplasmic domain of IgaA from Escherichia coli. Determined by X-ray diffraction at 2.64 Å resolution. Released 17 Jul 2024.

Method
X-ray diffraction
Resolution
2.64 Å
Organism
Escherichia coli
Chains
2
Atoms
4,049
Mol. weight
59.11 kDa
Released
17 Jul 2024

Explore 9BJ0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9BJ0 contains 28 α-helices and 18 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.

Chain A: 14 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand376-37941
α-helix382-3887
β-strand395-406121
β-strand423-43081
α-helix434-4396
α-helix442-45817
α-helix470-4789
β-strand482-48432
α-helix487-49711
α-helix505-5139
α-helix520-52910
β-strand537-53932
α-helix541-56929
α-helix573-5742
β-strand578-58251
α-helix591-5944
α-helix598-6003
α-helix603-6053
α-helix606-61712
β-strand620-633141
α-helix6381
β-strand639-64461
Chain B: 14 helices, 10 β-strands
ElementResiduesLengthSheet
β-strand376-37943
α-helix382-3865
β-strand395-40283
β-strand403-40644
β-strand423-43084
α-helix436-4394
α-helix442-45817
α-helix470-4789
β-strand482-48435
α-helix487-4959
α-helix505-51511
α-helix520-5289
β-strand537-53935
α-helix541-56929
α-helix573-5742
β-strand578-58254
α-helix591-5944
α-helix598-6003
α-helix603-6053
α-helix606-61712
β-strand620-62783
β-strand631-63334
α-helix6381
β-strand639-64354

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Intracellular growth attenuator protein igaAA, Bprotein274Escherichia coliP45800 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>9BJ0_1 Intracellular growth attenuator protein igaA (chains A, B)
SAQTIEATSVKQLADAGVRVGDTLRISGTGMCNIRTSGTWSAKTNSPFLPFDCSQIIWND
ARSLPLPESELVNKATALTEAVNRQLHPKPEDESRVSASLRSAIQKSGMVLLDDFGDIVL
KTADLCSAKDDCVRLKNALVNLGNSKDWDALVKRANAGKLDGVNVLLRPVSAESLDNLVA
TSTAPFITHETARAAQSLNSPAPGGFLIVSDEGSDFVDQPWPSASLYDYPPQEQWNAFQK
LAQMLMHTPFNAEGIVTKIFTDANGTQHIGLHPI

Primary citation

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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