Research workbench

Tail proteins

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

PDB: 7EY9
Type: protein
Length: 9,552 residues
Chains: 36
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tail fiber protein; Tail tubular protein GP12; Tail tubular protein GP11
UniProt: P03748, P03747, P03746
Pockets: 20 · best druggability 0.86

Structure

electron microscopy · 6 distinct chains · 16% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
a, d, g, j, m, p	Tail fiber protein	protein	141	21% helix, 23% strand	P03748
b, e, h, k, n, q	Tail fiber protein	protein	134	19% helix, 25% strand	P03748
c, f, i, l, o, r	Tail fiber protein	protein	136	13% helix, 23% strand	P03748
s, t, u, v, w, x	Tail tubular protein GP12	protein	792	5% helix, 40% strand	P03747
M, O, Q, S, U, W	Tail tubular protein GP11	protein	194	38% helix, 12% strand	P03746
N, P, R, T, V, X	Tail tubular protein GP11	protein	195	39% helix, 16% strand	P03746

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	968	0.86	0.88	114	empty
2	1051	0.86	0.87	129	empty
3	1083	0.86	0.87	130	empty
4	1083	0.86	0.87	130	empty
5	1115	0.85	0.86	127	empty

Interfaces

110 interfaces between chains.

v–w · 3787 Å² buried · 48 hydrogen bonds · protein-protein
t–u · 3785 Å² buried · 48 hydrogen bonds · protein-protein
s–x · 3784 Å² buried · 49 hydrogen bonds · protein-protein
u–v · 3775 Å² buried · 47 hydrogen bonds · protein-protein
s–t · 3774 Å² buried · 48 hydrogen bonds · protein-protein

Compared structures

7EY9 · tail proteins · 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 P03748
Every structure of UniProt P03747
Every structure of UniProt P03746
Elsewhere: RCSB PDB 7EY9 · PDBe 7EY9 · UniProt P03748 · UniProt P03747 · UniProt P03746

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