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Cryo-EM of form 1 related peptide filament, 36-31-3-rd

Analyse Cryo-EM of form 1 related peptide filament, 36-31-3-rd in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6WL0
Type: protein
Length: 1,476 residues
Chains: 41
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptide 36-31-3-rd
Pockets: 10 · best druggability 0.38

Structure

electron microscopy · 1 distinct chain · 94% helix, 0% 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, h, i, j, k, l, m, n, o	Peptide 36-31-3-rd	protein	36	94% helix, 0% strand	—

Pockets

10 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	115	0.38	0.74	33	empty
2	91	0.34	0.74	26	empty
3	93	0.34	0.74	25	empty
4	103	0.34	0.73	29	empty
5	64	0.32	0.76	19	empty

Interfaces

146 interfaces between chains.

U–a · 742 Å² buried · 1 hydrogen bond · protein-protein
i–o · 739 Å² buried · 2 hydrogen bonds · protein-protein
P–V · 736 Å² buried · 1 hydrogen bond · protein-protein
e–k · 735 Å² buried · 2 hydrogen bonds · protein-protein
W–c · 734 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

6WL0 · Cryo-EM of Form 1 related peptide filament, 36-31-3-RD · the same entry in another collection · chain N against N, 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
Elsewhere: RCSB PDB 6WL0 · PDBe 6WL0

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