Research workbench

Cryo-EM of the S. solfataricus pilus

Analyse Cryo-EM of the S. solfataricus pilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6W8X
Type: protein
Length: 4,356 residues
Chains: 33
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pilin
UniProt: A0A157T322
Pockets: 20 · best druggability 0.92

Structure

electron microscopy · 1 distinct chain · 27% helix, 42% 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, V, W, X, Y, Z, a, b, c, d, e, f, g	Pilin	protein	132	27% helix, 42% strand	A0A157T322

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	1166	0.92	0.95	240	empty
2	144	0.80	0.97	38	empty
3	136	0.80	0.97	37	empty
4	146	0.80	0.96	38	empty
5	135	0.79	0.96	36	empty

Interfaces

139 interfaces between chains.

B–M · 1035 Å² buried · 4 hydrogen bonds · protein-protein
J–X · 1030 Å² buried · 4 hydrogen bonds · protein-protein
I–W · 1026 Å² buried · 4 hydrogen bonds · protein-protein
A–N · 1024 Å² buried · 4 hydrogen bonds · protein-protein
C–Q · 1024 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

6W8X · Cryo-EM of the S. solfataricus pilus · the same entry in another collection · chain B against B, 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 A0A157T322
Elsewhere: RCSB PDB 6W8X · PDBe 6W8X · UniProt A0A157T322

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