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Crystal structure of NSP2 protease from chikungunya virus in P212121 space group at 2.59 a (4MOLECULES/ASU).

Analyse Crystal structure of NSP2 protease from chikungunya virus in P212121 space… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ZTB
Type: protein
Length: 1,284 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protease NSP2
UniProt: A6MH22
Pockets: 12 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Protease NSP2	protein	321	33% helix, 21% strand	A6MH22

Ligands and binding sites

GOL · Glycerol · additive · 10 copies · chains A, B, C, D

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

Pockets

12 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1092	0.85	0.86	126	GOL
2	1079	0.84	0.85	119	GOL
3	171	0.65	0.86	31	empty
4	120	0.63	0.87	22	empty
5	137	0.62	0.86	27	empty

Interfaces

3 interfaces between chains.

B–C · 964 Å² buried · 20 hydrogen bonds · protein-protein
A–D · 961 Å² buried · 18 hydrogen bonds · protein-protein
A–B · 944 Å² buried · 7 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 A6MH22
Elsewhere: RCSB PDB 4ZTB · PDBe 4ZTB · UniProt A6MH22

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