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Crystal structure of the asymmetric human metapneumovirus M2-1 tetramer, form 1
Analyse Crystal structure of the asymmetric human metapneumovirus M2-1 tetramer, form 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CS7
- Type
- protein
- Length
- 672 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- M2-1
- UniProt
- Q8QN58
- Ligands
- ZN
- Pockets
- 7 · best druggability 0.80
Structure
x-ray diffraction · 3 distinct chains · 65% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | M2-1 | protein | 166 | 69% helix, 2% strand | Q8QN58 |
| C | M2-1 | protein | 172 | 62% helix, 1% strand | Q8QN58 |
| E | M2-1 | protein | 168 | 65% 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
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 553 | 0.80 | 0.86 | 70 | empty |
| 2 | 849 | 0.79 | 0.82 | 82 | empty |
| 3 | 948 | 0.75 | 0.78 | 74 | empty |
| 4 | 282 | 0.63 | 0.81 | 40 | empty |
| 5 | 116 | 0.44 | 0.78 | 19 | empty |
Interfaces
6 interfaces between chains.
- A–E · 1952 Ų buried · 39 hydrogen bonds · protein-protein
- B–E · 1839 Ų buried · 31 hydrogen bonds · protein-protein
- A–C · 1677 Ų buried · 28 hydrogen bonds · protein-protein
- B–C · 792 Ų buried · 11 hydrogen bonds · protein-protein
- C–E · 591 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 4CS7 · Crystal structure of the asymmetric human metapneumovirus M2-1 tetramer, form 1 · 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 4CS7 · PDBe 4CS7 · UniProt Q8QN58
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