MolNFT v1 · #32510 · protein

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

2BSJ · Chaperone protein syct: “Native crystal structure of the type III secretion chaperone syct from yersinia enterocolitica”. X-ray diffraction, 1 ligand (CL), 2 pockets (best druggability 0.60). MolNFT v1 #32510 on GenesisL1: 3D…

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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