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Crystal structure of the protein secretion chaperone csaa from agrobacterium tumefaciens.

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: 2Q2I
Type: protein
Length: 221 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Secretion chaperone
UniProt: Q8UDB9
Ligands: SO4
Pockets: 2 · best druggability 0.48

Structure

x-ray diffraction · 2 distinct chains · 10% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Secretion chaperone	protein	112	12% helix, 41% strand	Q8UDB9
B	Secretion chaperone	protein	109	8% helix, 44% strand	Q8UDB9

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A
EDO · 1,2-ethanediol · additive · 5 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	156	0.48	0.77	29	SO4
2	58	0.29	0.74	13	EDO

Interfaces

1 interface between chains.

A–B · 1899 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

2Q2I · 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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Every structure of UniProt Q8UDB9
Elsewhere: RCSB PDB 2Q2I · PDBe 2Q2I · UniProt Q8UDB9

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