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Single particle cryoem structure of V. cholerae type IV competence pilus secretin pilq

Analyse Single particle cryoem structure of V. cholerae type IV competence pilus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6W6M
Type: protein
Length: 5,768 residues
Chains: 14
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Type IV pilus secretin pilq family protein
UniProt: A0A2V4P274
Pockets: 20 · best druggability 0.85

Structure

electron microscopy · 1 distinct chain · 19% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N	Type IV pilus secretin pilq family protein	protein	412	19% helix, 51% strand	A0A2V4P274

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1118	0.85	0.86	146	empty
2	497	0.76	0.83	70	empty
3	446	0.75	0.84	63	empty
4	451	0.75	0.84	61	empty
5	436	0.75	0.84	61	empty

Interfaces

15 interfaces between chains.

D–K · 4946 Å² buried · 54 hydrogen bonds · protein-protein
J–N · 4912 Å² buried · 55 hydrogen bonds · protein-protein
G–K · 4889 Å² buried · 56 hydrogen bonds · protein-protein
F–G · 4887 Å² buried · 56 hydrogen bonds · protein-protein
M–N · 4852 Å² buried · 53 hydrogen bonds · protein-protein

Compared structures

6W6M · Single particle cryoEM structure of V. cholerae Type IV competence pilus secretin PilQ · 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 A0A2V4P274
Elsewhere: RCSB PDB 6W6M · PDBe 6W6M · UniProt A0A2V4P274

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