Research workbench

Influenza virus (VN1194) H5 I155F mutant ha

Analyse Influenza virus (VN1194) H5 I155F mutant ha in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ZPA
Type: protein
Length: 479 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hemagglutinin
UniProt: Q6DQ34
Ligands: NAG
Pockets: 2 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 24% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	Hemagglutinin	protein	321	10% helix, 40% strand	Q6DQ34
F	Hemagglutinin	protein	158	54% helix, 15% strand	Q6DQ34

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains E

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

Pockets

2 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	293	0.59	0.78	43	empty
2	64	0.45	0.82	15	empty

Interfaces

1 interface between chains.

E–F · 2447 Å² buried · 37 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

3ZPA · INFLUENZA VIRUS (VN1194) H5 I155F mutant HA · the same entry in another collection · chain E against E, 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 Q6DQ34
Elsewhere: RCSB PDB 3ZPA · PDBe 3ZPA · UniProt Q6DQ34

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