Research workbench
Influenza virus (VN1194) H5 ha A138V mutant with lstc
Analyse Influenza virus (VN1194) H5 ha A138V mutant with lstc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZP3
- Type
- protein
- Length
- 479 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Haemagglutinin
- UniProt
- Q6DQ34
- Ligands
- NAG, SIA, GAL
- Pockets
- 4 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 24% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Haemagglutinin | protein | 321 | 9% helix, 42% strand | Q6DQ34 |
| F | Haemagglutinin | protein | 158 | 54% helix, 13% strand | Q6DQ34 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains E
- SIA · N-acetyl-alpha-neuraminic acid · sugar · chains E
- GAL · beta-D-galactopyranose · ion · chains E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 291 | 0.58 | 0.77 | 42 | empty |
| 2 | 61 | 0.39 | 0.80 | 13 | empty |
| 3 | 67 | 0.33 | 0.75 | 15 | empty |
| 4 | 76 | 0.31 | 0.74 | 17 | empty |
Interfaces
1 interface between chains.
- E–F · 2451 Ų buried · 36 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
- 3ZP3 · INFLUENZA VIRUS (VN1194) H5 HA A138V mutant with LSTc · 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 3ZP3 · PDBe 3ZP3 · UniProt Q6DQ34
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