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Native crystal structure of the type III secretion chaperone syct from yersinia enterocolitica

Analyse Native crystal structure of the type III secretion chaperone syct from yersinia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2BSJ
Type: protein
Length: 250 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chaperone protein syct
UniProt: O85243
Ligands: CL
Pockets: 2 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 26% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chaperone protein syct	protein	128	27% helix, 27% strand	O85243
B	Chaperone protein syct	protein	122	25% helix, 30% strand	O85243

Ligands and binding sites

CL · Chloride ion · ion · 2 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	322	0.60	0.78	42	empty
2	83	0.36	0.75	15	empty

Interfaces

1 interface between chains.

A–B · 1386 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

2BSJ · Native Crystal Structure of the Type III Secretion chaperone SycT from Yersinia… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt O85243
Elsewhere: RCSB PDB 2BSJ · PDBe 2BSJ · UniProt O85243

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