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Structure of CAE31940 from bordetella bronchiseptica RB50

Analyse Structure of CAE31940 from bordetella bronchiseptica RB50 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3QSL
Type: protein
Length: 644 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative exported protein
UniProt: Q7WME9
Pockets: 4 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative exported protein	protein	318	48% helix, 18% strand	Q7WME9
B	Putative exported protein	protein	326	48% helix, 18% strand	Q7WME9

Ligands and binding sites

CIT · Citric acid · additive · 2 copies · chains A, B

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

Pockets

4 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	274	0.60	0.79	29	empty
2	194	0.46	0.74	28	empty
3	63	0.38	0.79	16	empty
4	96	0.34	0.73	18	empty

Interfaces

1 interface between chains.

A–B · 505 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

3QSL · Structure of CAE31940 from Bordetella bronchiseptica RB50 · 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 Q7WME9
Elsewhere: RCSB PDB 3QSL · PDBe 3QSL · UniProt Q7WME9

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