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Crystal structure of PEB3 from campylobacter jejuni

Analyse Crystal structure of PEB3 from campylobacter jejuni in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2HXW
Type: protein
Length: 459 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Major antigenic peptide PEB3
UniProt: Q9PIK7
Pockets: 3 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Major antigenic peptide PEB3	protein	229	38% helix, 22% strand	Q9PIK7
B	Major antigenic peptide PEB3	protein	230	36% helix, 21% strand	Q9PIK7

Ligands and binding sites

FLC · Citrate anion · additive · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	106	0.59	0.87	24	empty
2	107	0.57	0.85	33	FLC
3	113	0.56	0.84	30	FLC

Interfaces

1 interface between chains.

A–B · 1851 Å² buried · 40 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

2HXW · Crystal Structure of Peb3 from Campylobacter jejuni · 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 Q9PIK7
Elsewhere: RCSB PDB 2HXW · PDBe 2HXW · UniProt Q9PIK7

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