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Structure of H2 japan hemagglutinin

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

PDB: 2WRD
Type: protein
Length: 1,439 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hemagglutinin
UniProt: Q67085
Pockets: 20 · best druggability 0.84

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hemagglutinin	protein	472	25% helix, 29% strand	Q67085
B	Hemagglutinin	protein	486	23% helix, 30% strand	Q67085
C	Hemagglutinin	protein	481	24% helix, 29% strand	Q67085

Pockets

20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1094	0.84	0.85	114	empty
2	160	0.83	0.98	24	empty
3	305	0.74	0.86	48	empty
4	228	0.73	0.88	36	empty
5	402	0.71	0.82	63	empty

Interfaces

3 interfaces between chains.

A–C · 2490 Å² buried · 42 hydrogen bonds · protein-protein
B–C · 2469 Å² buried · 36 hydrogen bonds · protein-protein
A–B · 2453 Å² buried · 41 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 disulfide (disulfide).

Compared structures

2WRD · structure of H2 japan 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
Every structure of UniProt Q67085
Elsewhere: RCSB PDB 2WRD · PDBe 2WRD · UniProt Q67085

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