Research workbench

AAV1 in complex with aavr

Analyse AAV1 in complex with aavr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6JCQ
Type: protein
Length: 609 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Capsid protein; Dyslexia-associated protein KIAA0319-like protein
UniProt: Q9WBP8, Q8IZA0
Pockets: 10 · best druggability 0.56

Structure

electron microscopy · 2 distinct chains · 3% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Capsid protein	protein	518	4% helix, 30% strand	Q9WBP8
R	Dyslexia-associated protein KIAA0319-like protein	protein	91	0% helix, 47% strand	Q8IZA0

Pockets

10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	245	0.56	0.77	38	empty
2	270	0.55	0.76	33	empty
3	178	0.44	0.74	23	empty
4	130	0.44	0.76	28	empty
5	171	0.43	0.74	26	empty

Interfaces

1 interface between chains.

A–R · 617 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

6JCQ · AAV1 in complex with AAVR · the same entry in another collection · chain A against A, TM-score 1.00
Q8IZA0 · AlphaFold monomer V2.0 prediction for dyslexia-associated protein KIAA0319-like protein… · a predicted model of the same protein · chain R against A, TM-score 0.91

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 Q9WBP8
Every structure of UniProt Q8IZA0
Elsewhere: RCSB PDB 6JCQ · PDBe 6JCQ · UniProt Q9WBP8 · UniProt Q8IZA0

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