Research workbench
Crystal structure of the asymmetric human metapneumovirus M2-1 tetramer bound to a DNA 4-mer
Analyse Crystal structure of the asymmetric human metapneumovirus M2-1 tetramer bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CSA
- Type
- protein + DNA
- Length
- 651 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- M2-1; 5'-D(*AP*GP*TP*TP*AP)-3'
- UniProt
- Q8QN58
- Ligands
- ZN
- Pockets
- 7 · best druggability 0.79
Structure
x-ray diffraction · 5 distinct chains · 68% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | M2-1 | protein | 161 | 70% helix, 1% strand | Q8QN58 |
| B | M2-1 | protein | 159 | 70% helix, 1% strand | Q8QN58 |
| C | M2-1 | protein | 164 | 68% helix, 1% strand | Q8QN58 |
| E | M2-1 | protein | 163 | 64% helix, 1% strand | Q8QN58 |
| G | 5'-D(*AP*GP*TP*TP*AP)-3' | dna | 4 | — | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 619 | 0.79 | 0.85 | 73 | empty |
| 2 | 284 | 0.77 | 0.90 | 42 | empty |
| 3 | 366 | 0.57 | 0.75 | 52 | empty |
| 4 | 213 | 0.56 | 0.79 | 22 | empty |
| 5 | 151 | 0.54 | 0.81 | 21 | empty |
Interfaces
7 interfaces between chains.
- B–E · 2371 Ų buried · 47 hydrogen bonds · protein-protein
- A–E · 1798 Ų buried · 36 hydrogen bonds · protein-protein
- A–C · 1738 Ų buried · 35 hydrogen bonds · protein-protein
- B–C · 860 Ų buried · 17 hydrogen bonds · protein-protein
- C–E · 707 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 4CSA · Crystal structure of the asymmetric human metapneumovirus M2-1 tetramer bound to a DNA… · 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 4CSA · PDBe 4CSA · UniProt Q8QN58
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