MolNFT v1 · #168586 · protein

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

6WL1 · Peptide 36-31-3: “Cryo-EM of form 1 related peptide filament, 36-31-3”. Electron microscopy, 9 pockets (best druggability 0.46). MolNFT v1 #168586 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6WL1
Type: protein
Length: 1,872 residues
Chains: 52
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptide 36-31-3
Pockets: 9 · best druggability 0.46

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, p, q, r, s, t, u, v, w, x, y, z	Peptide 36-31-3	protein	36	94% helix, 0% strand	—

Pockets

9 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	179	0.46	0.75	31	empty
2	184	0.44	0.74	30	empty
3	173	0.44	0.74	28	empty
4	186	0.43	0.73	33	empty
5	158	0.42	0.74	32	empty

Interfaces

190 interfaces between chains.

L–R · 997 Å² buried · 1 hydrogen bond · protein-protein
D–J · 996 Å² buried · 1 hydrogen bond · protein-protein
t–z · 995 Å² buried · 1 hydrogen bond · protein-protein
g–m · 995 Å² buried · 1 hydrogen bond · protein-protein
m–s · 995 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

6WL1 · Cryo-EM of Form 1 related peptide filament, 36-31-3 · 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
Elsewhere: RCSB PDB 6WL1 · PDBe 6WL1

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