MolNFT v1 · #88357 · protein
Crystal structure of the asymmetric human metapneumovirus M2-1 tetramer, form 2
4CS8: “Crystal structure of the asymmetric human metapneumovirus M2-1 tetramer, form 2”. X-ray diffraction, 1 ligand (ZN), 10 pockets (best druggability 0.80). MolNFT v1 #88357 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4CS8
- Type
- protein
- Length
- 646 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- M2-1
- UniProt
- Q8QN58
- Ligands
- ZN
- Pockets
- 10 · best druggability 0.80
Structure
x-ray diffraction · 4 distinct chains · 69% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | M2-1 | protein | 159 | 70% helix, 1% strand | Q8QN58 |
| B | M2-1 | protein | 164 | 70% helix, 2% strand | Q8QN58 |
| C | M2-1 | protein | 162 | 67% helix, 1% strand | Q8QN58 |
| E | M2-1 | protein | 161 | 68% helix, 1% strand | Q8QN58 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A, B, C, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 458 | 0.80 | 0.88 | 58 | empty |
| 2 | 304 | 0.79 | 0.90 | 48 | empty |
| 3 | 292 | 0.64 | 0.81 | 27 | empty |
| 4 | 300 | 0.58 | 0.77 | 45 | empty |
| 5 | 62 | 0.52 | 0.86 | 21 | empty |
Interfaces
6 interfaces between chains.
- B–E · 2472 Ų buried · 35 hydrogen bonds · protein-protein
- A–E · 1833 Ų buried · 40 hydrogen bonds · protein-protein
- A–C · 1749 Ų buried · 30 hydrogen bonds · protein-protein
- B–C · 837 Ų buried · 12 hydrogen bonds · protein-protein
- C–E · 736 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 4CS8 · Crystal structure of the asymmetric human metapneumovirus M2-1 tetramer, form 2 · 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 Q8QN58
- Elsewhere: RCSB PDB 4CS8 · PDBe 4CS8 · UniProt Q8QN58
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