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The structure of vaccina virus H7 protein displays a novel phosphoinositide binding fold required for membrane biogenesis

Analyse The structure of vaccina virus H7 protein displays a novel phosphoinositide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4W60
Type: protein
Length: 463 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Late protein H7
UniProt: P08586
Pockets: 1 · best druggability 0.74

Structure

x-ray diffraction · 3 distinct chains · 55% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Late protein H7	protein	117	55% helix, 13% strand	P08586
B, C	Late protein H7	protein	116	55% helix, 13% strand	P08586
D	Late protein H7	protein	114	56% helix, 13% strand	P08586

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1058	0.74	0.77	89	empty

Interfaces

4 interfaces between chains.

B–C · 387 Å² buried · 1 hydrogen bond · protein-protein
B–D · 196 Å² buried · 3 hydrogen bonds · protein-protein
A–C · 162 Å² buried · 3 hydrogen bonds · protein-protein
C–D · 84 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

4W60 · The structure of Vaccina virus H7 protein displays A Novel Phosphoinositide binding fold… · 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 P08586
Elsewhere: RCSB PDB 4W60 · PDBe 4W60 · UniProt P08586

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