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Structure function studies of vaccinia virus host-range protein K1 reveal a novel ankyrin repeat interaction surface for K1S function

Analyse Structure function studies of vaccinia virus host-range protein K1 reveal a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3KEA
Type: protein
Length: 566 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: K1L
UniProt: Q6IV60
Pockets: 5 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 57% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	K1L	protein	283	57% helix, 1% strand	Q6IV60

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	506	0.64	0.77	63	empty
2	509	0.64	0.76	50	empty
3	91	0.38	0.77	22	empty
4	90	0.35	0.74	17	empty
5	73	0.32	0.74	17	empty

Interfaces

1 interface between chains.

A–B · 1113 Å² buried · 22 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 modified (engineered).

Compared structures

3KEA · Structure function studies of vaccinia virus host-range protein K1 reveal a novel ankyrin… · 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 Q6IV60
Elsewhere: RCSB PDB 3KEA · PDBe 3KEA · UniProt Q6IV60

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