Research workbench

The structure of influenza H2 human singapore hemagglutinin

Analyse The structure of influenza H2 human singapore hemagglutinin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WRC
Type: protein
Length: 1,427 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hemagglutinin
Pockets: 20 · best druggability 0.82

Structure

x-ray diffraction · 3 distinct chains · 24% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hemagglutinin	protein	474	24% helix, 27% strand	—
B	Hemagglutinin	protein	486	24% helix, 29% strand	—
C	Hemagglutinin	protein	467	23% helix, 30% strand	—

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	148	0.82	0.98	24	empty
2	347	0.74	0.86	47	empty
3	395	0.74	0.84	49	empty
4	693	0.73	0.80	55	empty
5	436	0.73	0.83	55	empty

Interfaces

3 interfaces between chains.

A–B · 2471 Å² buried · 40 hydrogen bonds · protein-protein
A–C · 2468 Å² buried · 38 hydrogen bonds · protein-protein
B–C · 2448 Å² buried · 37 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 17 disulfide (disulfide).

Compared structures

2WRC · the structure of influenza H2 human singapore hemagglutinin · 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
Elsewhere: RCSB PDB 2WRC · PDBe 2WRC

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.