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Cryo-EM structure of the T4 tail tube

Analyse Cryo-EM structure of the T4 tail tube in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5W5F
Type: protein
Length: 2,934 residues
Chains: 18
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tail tube protein GP19
UniProt: P13333
Pockets: 20 · best druggability 0.49

Structure

electron microscopy · 1 distinct chain · 17% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, R, C, B, D, E, F, G, H, I, J, K, L, M, N, O, P, Q	Tail tube protein GP19	protein	163	17% helix, 47% strand	P13333

Pockets

20 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	192	0.49	0.75	19	empty
2	169	0.48	0.76	18	empty
3	186	0.48	0.75	19	empty
4	174	0.47	0.75	18	empty
5	169	0.46	0.75	18	empty

Interfaces

96 interfaces between chains.

J–M · 2280 Å² buried · 33 hydrogen bonds · protein-protein
F–I · 2276 Å² buried · 37 hydrogen bonds · protein-protein
C–Q · 2275 Å² buried · 36 hydrogen bonds · protein-protein
E–H · 2275 Å² buried · 36 hydrogen bonds · protein-protein
G–J · 2275 Å² buried · 37 hydrogen bonds · protein-protein

Compared structures

5W5F · Cryo-EM structure of the T4 tail tube · 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 P13333
Elsewhere: RCSB PDB 5W5F · PDBe 5W5F · UniProt P13333

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