MolNFT v1 · #35445 · protein

Core structure of GP2 from ebola virus

2EBO · Ebola virus envelope glycoprotein: “Core structure of GP2 from ebola virus”. X-ray diffraction, 1 ligand (CL), 1 pocket (best druggability 0.67). MolNFT v1 #35445 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2EBO
Type: protein
Length: 222 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ebola virus envelope glycoprotein
UniProt: Q05320
Ligands: CL
Pockets: 1 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 82% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Ebola virus envelope glycoprotein	protein	74	82% helix, 0% strand	Q05320

Ligands and binding sites

CL · Chloride ion · ion · chains A, B, C

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

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	72	0.67	0.94	17	empty

Interfaces

3 interfaces between chains.

A–B · 1385 Å² buried · 15 hydrogen bonds · protein-protein
B–C · 1356 Å² buried · 12 hydrogen bonds · protein-protein
A–C · 1351 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

2EBO · Core structure of GP2 from ebola virus · 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 Q05320
Elsewhere: RCSB PDB 2EBO · PDBe 2EBO · UniProt Q05320

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