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Crystal structure of cypovirus polyhedra mutant with deletion of GLY192-ALA194

Analyse Crystal structure of cypovirus polyhedra mutant with deletion of GLY192-ALA194 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5GQK
Type: protein
Length: 244 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Polyhedrin
UniProt: P11041
Ligands: ACE, CL
Pockets: 5 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Polyhedrin	protein	244	25% helix, 29% strand	P11041

Ligands and binding sites

ACE · Acetyl group · ligand · chains A
CL · Chloride ion · ion · chains A
EDO · 1,2-ethanediol · additive · 4 copies · chains A

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

Pockets

5 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	147	0.52	0.80	24	EDO
2	55	0.30	0.76	11	empty
3	58	0.30	0.75	18	empty
4	60	0.28	0.73	12	empty
5	53	0.27	0.74	13	empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

5GQK · Crystal structure of Cypovirus Polyhedra mutant with deletion of Gly192-Ala194 · 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 P11041
Elsewhere: RCSB PDB 5GQK · PDBe 5GQK · UniProt P11041

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