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Crystal structure of the protein secretion chaperone csaa from agrobacterium tumefaciens with a genetically fused phage-display derived peptide substrate at the N-terminus.

Analyse Crystal structure of the protein secretion chaperone csaa from agrobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2Q2H
Type
protein
Length
224 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Secretion chaperone, phage-display derived peptide
UniProt
Q8UDB9
Pockets
2 · best druggability 0.51

Structure

x-ray diffraction · 2 distinct chains · 10% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASecretion chaperone, phage-display derived peptideprotein11811% helix, 39% strandQ8UDB9
BSecretion chaperone, phage-display derived peptideprotein1068% helix, 43% strandQ8UDB9

Ligands and binding sites

  • ACT · Acetate ion · additive · 2 copies · chains A, B
  • CIT · Citric acid · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11850.510.7829ACT
2520.260.7413empty

Interfaces

1 interface between chains.

  • A–B · 1838 Ų buried · 19 hydrogen bonds · protein-protein

Compared structures

  • 2Q2H · Crystal structure of the protein secretion chaperone CsaA from Agrobacterium tumefaciens… · the same entry in another collection · chain A against A, TM-score 1.00

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