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Crystal structure of a secretion chaperone csaa from bacillus subtilis in the space group P 4 21 2

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

PDB
2NZH
Type
protein
Length
218 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein csaa
UniProt
P37584
Pockets
2 · best druggability 0.51

Structure

x-ray diffraction · 2 distinct chains · 14% helix, 45% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein csaaprotein11015% helix, 47% strandP37584
BProtein csaaprotein10813% helix, 43% strandP37584

Ligands and binding sites

  • GOL · Glycerol · 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
11900.510.7730empty
21510.470.7727empty

Interfaces

1 interface between chains.

  • A–B · 1563 Ų buried · 26 hydrogen bonds · protein-protein

Compared structures

  • 2NZH · Crystal structure of a secretion chaperone CsaA from Bacillus subtilis in the space group… · the same entry in another collection · chain A against A, TM-score 1.00
  • P37584 · AlphaFold monomer V2.0 prediction for probable chaperone csaa (P37584) · a predicted model of the same protein · chain B against A, TM-score 0.99

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