MolNFT v2 · #208483 · protein

Cryo-EM reconstruction of the CS17 bacterial adhesion pili

8EHS · CS17 fimbriae major subunit: “Cryo-EM reconstruction of the CS17 bacterial adhesion pili”. Electron microscopy at 3.3, 7 pockets (best druggability 0.79). MolNFT v2 #208483 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 8EHS
Type: protein
Length: 1,015 residues
Chains: 7
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.3
Source: Escherichia coli
Molecule: CS17 fimbriae major subunit
UniProt: Q848J7
Pockets: 7 · best druggability 0.79

Structure

electron microscopy · resolution 3.3 · 1 distinct chain · 2% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
G, A, B, C, D, E, F	CS17 fimbriae major subunit	protein	145	2% helix, 46% strand	Q848J7

Pockets

7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1187	0.79	0.81	102	empty
2	1070	0.77	0.80	106	empty
3	935	0.77	0.80	97	empty
4	919	0.77	0.80	96	empty
5	116	0.56	0.84	26	empty

Interfaces

18 interfaces between chains.

B–C · 1322 Å² buried · 26 hydrogen bonds · protein-protein
E–F · 1315 Å² buried · 27 hydrogen bonds · protein-protein
A–B · 1308 Å² buried · 26 hydrogen bonds · protein-protein
G–A · 1306 Å² buried · 31 hydrogen bonds · protein-protein
C–D · 1305 Å² buried · 28 hydrogen bonds · protein-protein

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 Q848J7
Elsewhere: RCSB PDB 8EHS · PDBe 8EHS · UniProt Q848J7

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