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Structure of the tir-cest effector-chaperone complex

Analyse Structure of the tir-cest effector-chaperone complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5WEZ
Type
protein
Length
159 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tir chaperone; Translocated intimin receptor tir
UniProt
P21244, B7UM99

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATir chaperoneprotein12937% helix, 27% strandP21244
BTranslocated intimin receptor tirprotein300% helix, 17% strandB7UM99

Interfaces

1 interface between chains.

  • A–B · 1198 Ų buried · 18 hydrogen bonds · protein-protein

Compared structures

  • 5WEZ · Structure of the Tir-CesT effector-chaperone complex · the same entry in another collection · chain A against A, TM-score 1.00
  • P21244 · AlphaFold monomer V2.0 prediction for tir chaperone (P21244) · a predicted model of the same protein · chain A against A, TM-score 0.96
  • B7UM99 · AlphaFold monomer V2.0 prediction for translocated intimin receptor tir (B7UM99) · a predicted model of the same protein · chain B against A, TM-score 0.28

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