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Canine adenovirus fibre head at 1.5 a resolution

Analyse Canine adenovirus fibre head at 1.5 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2J2J
Type: protein
Length: 1,092 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fiber protein
UniProt: Q65914
Pockets: 12 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Fiber protein	protein	182	8% helix, 45% strand	Q65914

Pockets

12 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	704	0.83	0.87	67	empty
2	709	0.83	0.87	68	empty
3	304	0.67	0.82	42	empty
4	186	0.61	0.83	27	empty
5	187	0.60	0.82	27	empty

Interfaces

9 interfaces between chains.

B–D · 1183 Å² buried · 22 hydrogen bonds · protein-protein
C–F · 1169 Å² buried · 23 hydrogen bonds · protein-protein
E–F · 1168 Å² buried · 23 hydrogen bonds · protein-protein
C–E · 1168 Å² buried · 21 hydrogen bonds · protein-protein
A–B · 1166 Å² buried · 22 hydrogen bonds · protein-protein

Compared structures

2J2J · Canine adenovirus fibre head at 1.5 A resolution · 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 Q65914
Elsewhere: RCSB PDB 2J2J · PDBe 2J2J · UniProt Q65914

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