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Structure of rabies virus glycoprotein in complex with neutralizing antibody 523-11 at acidic pH

Analyse Structure of rabies virus glycoprotein in complex with neutralizing antibody… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6LGW
Type: protein
Length: 1,191 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Scfv 523-11 vh; Scfv 523-11 vl; GLYCOPROTEIN,GLYCOPROTEIN,GLYCOPROTEIN
UniProt: Q5JZZ2, Q2Z2I1, D8VEC1
Pockets: 19 · best druggability 0.78

Structure

x-ray diffraction · 5 distinct chains · 14% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Scfv 523-11 vh	protein	118	8% helix, 55% strand	—
B, D	Scfv 523-11 vl	protein	104	3% helix, 45% strand	—
E	GLYCOPROTEIN,GLYCOPROTEIN,GLYCOPROTEIN	protein	368	17% helix, 35% strand	Q5JZZ2, Q2Z2I1, D8VEC1
C	Scfv 523-11 vh	protein	119	5% helix, 54% strand	—
F	GLYCOPROTEIN,GLYCOPROTEIN,GLYCOPROTEIN	protein	378	19% helix, 33% strand	Q5JZZ2, Q2Z2I1, D8VEC1

Pockets

19 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1134	0.78	0.80	77	empty
2	134	0.68	0.89	32	empty
3	459	0.66	0.78	51	empty
4	309	0.65	0.81	45	empty
5	382	0.64	0.79	43	empty

Interfaces

7 interfaces between chains.

E–F · 1340 Å² buried · 19 hydrogen bonds · protein-protein
C–F · 939 Å² buried · 14 hydrogen bonds · protein-protein
A–E · 818 Å² buried · 18 hydrogen bonds · protein-protein
A–B · 795 Å² buried · 11 hydrogen bonds · protein-protein
C–D · 782 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 disulfide (disulfide).

Compared structures

6LGW · Structure of Rabies virus glycoprotein in complex with neutralizing antibody 523-11 at… · 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 Q5JZZ2
Every structure of UniProt Q2Z2I1
Every structure of UniProt D8VEC1
Elsewhere: RCSB PDB 6LGW · PDBe 6LGW · UniProt Q5JZZ2 · UniProt Q2Z2I1 · UniProt D8VEC1

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