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X-ray structure of a human kobuvirus: aichi virus a (aiv)

Analyse X-ray structure of a human kobuvirus: aichi virus a (aiv) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5AOO
Type: protein
Length: 763 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: VP0; VP1; VP3
UniProt: Q91QP4
Pockets: 7 · best druggability 0.58

Structure

x-ray diffraction · 3 distinct chains · 9% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	VP0	protein	229	9% helix, 37% strand	Q91QP4
B	VP1	protein	314	10% helix, 33% strand	Q91QP4
C	VP3	protein	220	8% helix, 38% strand	Q91QP4

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	64	0.58	0.89	23	empty
2	172	0.49	0.77	28	empty
3	142	0.46	0.77	25	empty
4	92	0.42	0.78	18	empty
5	92	0.39	0.77	21	empty

Interfaces

3 interfaces between chains.

A–C · 2917 Å² buried · 41 hydrogen bonds · protein-protein
A–B · 2382 Å² buried · 34 hydrogen bonds · protein-protein
B–C · 2268 Å² buried · 35 hydrogen bonds · protein-protein

Compared structures

5AOO · X-ray structure of a human Kobuvirus: Aichi virus A (AiV) · 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 Q91QP4
Elsewhere: RCSB PDB 5AOO · PDBe 5AOO · UniProt Q91QP4

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