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2.1 ångström resolution crystal structure of matrix protein 1 (M1; residues 1-164) from influenza a virus (A/PUERTO RICO/8/34(H1N1))
Analyse 2.1 ångström resolution crystal structure of matrix protein 1 (M1; residues… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CQE
- Type
- protein
- Length
- 319 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Matrix protein 1
- UniProt
- P03485
- Ligands
- CL
- Pockets
- 2 · best druggability 0.36
Structure
x-ray diffraction · 2 distinct chains · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Matrix protein 1 | protein | 158 | 67% helix, 0% strand | P03485 |
| B | Matrix protein 1 | protein | 161 | 68% helix, 0% strand | P03485 |
Ligands and binding sites
- CL · Chloride ion · ion · 3 copies · chains A, B
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
- EDO · 1,2-ethanediol · additive · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 90 | 0.36 | 0.75 | 15 | empty |
| 2 | 84 | 0.35 | 0.75 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1182 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 5CQE · 2.1 Angstrom resolution crystal structure of matrix protein 1 (M1; residues 1-164) from… · 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 P03485
- Elsewhere: RCSB PDB 5CQE · PDBe 5CQE · UniProt P03485
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