Research workbench

Cryo-EM reconstruction of sulfolobus islandicus LAL14/1 pilus

Analyse Cryo-EM reconstruction of sulfolobus islandicus LAL14/1 pilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6NAV
Type: protein
Length: 2,751 residues
Chains: 21
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: M9UD72
UniProt: M9UD72
Pockets: 20 · best druggability 0.81

Structure

electron microscopy · 1 distinct chain · 27% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U	M9UD72	protein	131	27% helix, 37% strand	M9UD72

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	190	0.81	0.95	41	empty
2	121	0.78	0.96	26	empty
3	107	0.77	0.97	21	empty
4	120	0.76	0.95	25	empty
5	111	0.76	0.96	22	empty

Interfaces

98 interfaces between chains.

C–L · 1012 Å² buried · 7 hydrogen bonds · protein-protein
C–Q · 1009 Å² buried · 7 hydrogen bonds · protein-protein
D–K · 1009 Å² buried · 7 hydrogen bonds · protein-protein
G–U · 1009 Å² buried · 7 hydrogen bonds · protein-protein
E–J · 1009 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

6NAV · Cryo-EM reconstruction of Sulfolobus islandicus LAL14/1 Pilus · 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 M9UD72
Elsewhere: RCSB PDB 6NAV · PDBe 6NAV · UniProt M9UD72

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