MolNFT v1 · #113794 · protein

Structure of the carboxy-terminal domain of the bacteriophage T5 L- shaped tail fibre

5AQ5 · L-shaped tail fiber protein PB8: “Structure of the carboxy-terminal domain of the bacteriophage T5 L- shaped tail fibre”. X-ray diffraction, 20 pockets (best druggability 0.86). MolNFT v1 #113794 on GenesisL1: 3D structure, binding…

PDB: 5AQ5
Type: protein
Length: 3,302 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: L-shaped tail fiber protein PB8
UniProt: Q66LT2
Pockets: 20 · best druggability 0.86

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D, E, F, G, H, I, J, K, L	L-shaped tail fiber protein PB8	protein	275	7% helix, 41% strand	Q66LT2
B, C	L-shaped tail fiber protein PB8	protein	276	7% helix, 41% strand	Q66LT2

Pockets

20 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1015	0.86	0.87	129	empty
2	50	0.72	0.99	20	empty
3	458	0.64	0.77	51	empty
4	465	0.63	0.77	64	empty
5	400	0.61	0.77	60	empty

Interfaces

39 interfaces between chains.

A–B · 6313 Å² buried · 117 hydrogen bonds · protein-protein
B–C · 6305 Å² buried · 120 hydrogen bonds · protein-protein
G–H · 6263 Å² buried · 118 hydrogen bonds · protein-protein
D–F · 6259 Å² buried · 117 hydrogen bonds · protein-protein
J–K · 6254 Å² buried · 115 hydrogen bonds · protein-protein

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 Q66LT2
Elsewhere: RCSB PDB 5AQ5 · PDBe 5AQ5 · UniProt Q66LT2

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