Research workbench

VP16-VP17 complex, a complex of the two major capsid proteins of bacteriophage P23-77

Analyse VP16-VP17 complex, a complex of the two major capsid proteins of bacteriophage… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ZN6
Type: protein
Length: 366 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: VP17; VP16
UniProt: C8CHL5, C8CHL4
Ligands: NA, CL
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	VP17	protein	221	4% helix, 47% strand	C8CHL5
B	VP16	protein	145	11% helix, 37% strand	C8CHL4

Ligands and binding sites

NA · Sodium ion · metal · chains B
CL · Chloride ion · ion · chains B

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

Pockets

2 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	854	0.74	0.78	77	empty
2	188	0.72	0.89	24	empty

Interfaces

1 interface between chains.

A–B · 786 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

3ZN6 · VP16-VP17 complex, a complex of the two major capsid proteins of bacteriophage P23-77 · 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 C8CHL5
Every structure of UniProt C8CHL4
Elsewhere: RCSB PDB 3ZN6 · PDBe 3ZN6 · UniProt C8CHL5 · UniProt C8CHL4

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