Research workbench

Cryo-EM reconstruction of CFA/I pili

Analyse Cryo-EM reconstruction of CFA/I pili in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6NRV
Type: protein
Length: 1,898 residues
Chains: 13
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CFA/I fimbrial subunit B
UniProt: P0CK93
Pockets: 20 · best druggability 0.78

Structure

electron microscopy · 1 distinct chain · 2% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M	CFA/I fimbrial subunit B	protein	146	2% helix, 40% strand	P0CK93

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	1049	0.78	0.80	106	empty
2	724	0.76	0.81	98	empty
3	729	0.76	0.81	93	empty
4	77	0.74	0.97	26	empty
5	420	0.74	0.84	52	empty

Interfaces

42 interfaces between chains.

G–I · 1328 Å² buried · 25 hydrogen bonds · protein-protein
D–F · 1323 Å² buried · 23 hydrogen bonds · protein-protein
C–E · 1312 Å² buried · 22 hydrogen bonds · protein-protein
A–C · 1308 Å² buried · 23 hydrogen bonds · protein-protein
F–H · 1307 Å² buried · 24 hydrogen bonds · protein-protein

Compared structures

6NRV · Cryo-EM reconstruction of CFA/I pili · the same entry in another collection · chain K against K, 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 P0CK93
Elsewhere: RCSB PDB 6NRV · PDBe 6NRV · UniProt P0CK93

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.