Research workbench
Human antibody H2526 in complex with influenza hemagglutinin H1 solomon ISLANDS/03/2006
Analyse Human antibody H2526 in complex with influenza hemagglutinin H1 solomon… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4YJZ
- Type
- protein
- Length
- 446 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemagglutinin; Scfv H2526
- UniProt
- A7UPX0
- Ligands
- NAG
- Pockets
- 5 · best druggability 0.54
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Hemagglutinin | protein | 212 | 11% helix, 39% strand | A7UPX0 |
| L | Scfv H2526 | protein | 234 | 8% helix, 48% strand | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains E, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 92 | 0.54 | 0.84 | 17 | empty |
| 2 | 65 | 0.47 | 0.84 | 19 | empty |
| 3 | 126 | 0.43 | 0.77 | 31 | empty |
| 4 | 97 | 0.36 | 0.74 | 21 | empty |
| 5 | 58 | 0.28 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- E–L · 967 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide, 3 glycan (disulfide, N-glycosylation).
Compared structures
- 4YJZ · Human antibody H2526 in complex with influenza hemagglutinin H1 Solomon Islands/03/2006 · 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 A7UPX0
- Elsewhere: RCSB PDB 4YJZ · PDBe 4YJZ · UniProt A7UPX0
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