MolNFT v1 · #159978 · protein
Crystal structure of the cedar henipavirus attachment G glycoprotein global domain
6P72 · Attachment glycoprotein: “Crystal structure of the cedar henipavirus attachment G glycoprotein global domain”. X-ray diffraction, 3 ligands (NAG, MAN, BMA), 8 pockets (best druggability 0.71). MolNFT v1 #159978 on GenesisL1: 3D…
- PDB
- 6P72
- Type
- protein
- Length
- 852 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Attachment glycoprotein
- UniProt
- J7H333
- Ligands
- NAG, MAN, BMA
- Pockets
- 8 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Attachment glycoprotein | protein | 426 | 6% helix, 47% strand | J7H333 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 23 copies · chains A, C
- MAN · alpha-D-mannopyranose · sugar · 3 copies · chains A
- BMA · beta-D-mannopyranose · sugar · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 629 | 0.71 | 0.79 | 48 | empty |
| 2 | 583 | 0.68 | 0.78 | 40 | empty |
| 3 | 59 | 0.67 | 0.96 | 23 | empty |
| 4 | 136 | 0.51 | 0.80 | 22 | empty |
| 5 | 142 | 0.44 | 0.76 | 23 | empty |
Interfaces
1 interface between chains.
- A–C · 620 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 disulfide, 14 glycan (disulfide, N-glycosylation).
Compared structures
- 6P72 · Crystal Structure of the Cedar henipavirus Attachment G Glycoprotein global domain · 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 J7H333
- Elsewhere: RCSB PDB 6P72 · PDBe 6P72 · UniProt J7H333
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