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Endophilin B1 helical scaffold

Analyse Endophilin B1 helical scaffold in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6UP6
Type: protein
Length: 10,692 residues
Chains: 44
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endophilin-B1
UniProt: Q9Y371
Pockets: 20 · best druggability 0.82

Structure

electron microscopy · 1 distinct chain · 61% 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, V, W, a, b, c, d, e, f, g, h, i, j, k, l, m, n, o, p, q, r, s, t, v, w	Endophilin-B1	protein	243	61% helix, 0% strand	Q9Y371

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	867	0.82	0.84	97	empty
2	854	0.81	0.83	105	empty
3	818	0.81	0.83	91	empty
4	778	0.81	0.84	88	empty
5	763	0.81	0.84	88	empty

Interfaces

98 interfaces between chains.

K–L · 2929 Å² buried · 21 hydrogen bonds · protein-protein
o–p · 2925 Å² buried · 21 hydrogen bonds · protein-protein
e–f · 2925 Å² buried · 21 hydrogen bonds · protein-protein
A–B · 2924 Å² buried · 21 hydrogen bonds · protein-protein
Q–R · 2923 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

6UP6 · Endophilin B1 helical scaffold · 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 Q9Y371
Elsewhere: RCSB PDB 6UP6 · PDBe 6UP6 · UniProt Q9Y371

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