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Crystal structure of MERS-cov 3CL protease (C148A) in spacegroup P212121,PH 9.0

Analyse Crystal structure of MERS-cov 3CL protease (C148A) in spacegroup P212121,PH 9.0 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7DRA
Type: protein
Length: 565 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3C-like proteinase
EC: 3.4.22.69
UniProt: T2B9I2
Pockets: 5 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 25% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3C-like proteinase (EC 3.4.22.69)	protein	279	25% helix, 31% strand	T2B9I2
B	3C-like proteinase (EC 3.4.22.69)	protein	286	25% helix, 30% strand	T2B9I2

Pockets

5 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	924	0.75	0.79	96	empty
2	299	0.55	0.75	43	empty
3	138	0.38	0.73	20	empty
4	73	0.34	0.76	14	empty
5	95	0.33	0.73	21	empty

Interfaces

1 interface between chains.

A–B · 888 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

7DRA · Crystal structure of MERS-CoV 3CL protease (C148A) in spacegroup P212121,pH 9.0 · 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 T2B9I2
Elsewhere: RCSB PDB 7DRA · PDBe 7DRA · UniProt T2B9I2

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