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Complex structure of pedv 3CLPRO mutant (C144A) with a peptide substrate.

Analyse Complex structure of pedv 3CLPRO mutant (C144A) with a peptide substrate. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ZUH
Type: protein
Length: 600 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pedv 3C-like protease; Peptide substrate savlqsgf
UniProt: K4L9I6
Pockets: 4 · best druggability 0.76

Structure

x-ray diffraction · 3 distinct chains · 24% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pedv 3C-like protease	protein	298	24% helix, 30% strand	K4L9I6
B	Pedv 3C-like protease	protein	294	25% helix, 30% strand	K4L9I6
C	Peptide substrate savlqsgf	protein	8	0% helix, 38% strand	—

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	890	0.76	0.80	84	empty
2	278	0.59	0.79	40	empty
3	265	0.59	0.79	37	empty
4	177	0.46	0.75	28	empty

Interfaces

3 interfaces between chains.

A–B · 1386 Å² buried · 32 hydrogen bonds · protein-protein
A–C · 684 Å² buried · 15 hydrogen bonds · protein-protein
B–C · 16 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

4ZUH · Complex structure of PEDV 3CLpro mutant (C144A) with a peptide substrate. · the same entry in another collection · chain A against A, TM-score 1.00

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Every structure of UniProt K4L9I6
Elsewhere: RCSB PDB 4ZUH · PDBe 4ZUH · UniProt K4L9I6

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