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Ebola virus nucleoprotein bound to VP35 chaperoning peptide P212121

Analyse Ebola virus nucleoprotein bound to VP35 chaperoning peptide P212121 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ZTI
Type: protein
Length: 673 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Polymerase cofactor VP35,NUCLEOPROTEIN
UniProt: Q05127, P18272
Pockets: 9 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 61% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Polymerase cofactor VP35,NUCLEOPROTEIN	protein	336	61% helix, 7% strand	Q05127, P18272
B	Polymerase cofactor VP35,NUCLEOPROTEIN	protein	337	61% helix, 7% strand	Q05127, P18272

Pockets

9 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	960	0.79	0.81	103	empty
2	140	0.48	0.78	21	empty
3	134	0.43	0.76	22	empty
4	88	0.40	0.78	24	empty
5	53	0.40	0.81	17	empty

Interfaces

1 interface between chains.

A–B · 1365 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

4ZTI · Ebola virus nucleoprotein bound to VP35 chaperoning peptide P212121 · 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 Q05127
Every structure of UniProt P18272
Elsewhere: RCSB PDB 4ZTI · PDBe 4ZTI · UniProt Q05127 · UniProt P18272

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