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Crystal structure of C-terminal truncated (110-265) aura virus capsid protease.

Analyse Crystal structure of C-terminal truncated (110-265) aura virus capsid protease. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4UON
Type: protein
Length: 306 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Capsid protease
EC: 3.4.21.90
UniProt: Q86925
Pockets: 6 · best druggability 0.39

Structure

x-ray diffraction · 2 distinct chains · 9% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Capsid protease (EC 3.4.21.90)	protein	154	8% helix, 47% strand	Q86925
B	Capsid protease (EC 3.4.21.90)	protein	152	11% helix, 47% strand	Q86925

Ligands and binding sites

GOL · Glycerol · additive · 6 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

6 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	73	0.39	0.77	16	empty
2	62	0.36	0.78	19	GOL
3	72	0.34	0.75	12	empty
4	64	0.32	0.76	17	empty
5	66	0.32	0.76	18	GOL

Interfaces

1 interface between chains.

A–B · 390 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

4UON · Crystal structure of C-terminal truncated (110-265) Aura virus capsid protease. · 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 Q86925
Elsewhere: RCSB PDB 4UON · PDBe 4UON · UniProt Q86925

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