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Crystal structure of flgn chaperone from bordetella pertussis

Analyse Crystal structure of flgn chaperone from bordetella pertussis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3OPC
Type: protein
Length: 259 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
UniProt: Q7VYH2
Pockets: 3 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 90% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein	protein	128	90% helix, 0% strand	Q7VYH2
B	Uncharacterized protein	protein	131	90% helix, 0% strand	Q7VYH2

Ligands and binding sites

GOL · Glycerol · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	281	0.77	0.90	33	empty
2	100	0.36	0.74	16	GOL
3	90	0.34	0.74	16	empty

Interfaces

1 interface between chains.

A–B · 4076 Å² buried · 36 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

3OPC · Crystal structure of FlgN chaperone from Bordetella pertussis · 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 Q7VYH2
Elsewhere: RCSB PDB 3OPC · PDBe 3OPC · UniProt Q7VYH2

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