Research workbench
High resolution structure of mutant CA09-PB2CAP
Analyse High resolution structure of mutant CA09-PB2CAP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WOP
- Type
- protein
- Length
- 318 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polymerase PB2
- UniProt
- F4MEU3
- Pockets
- 3 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Polymerase PB2 | protein | 159 | 23% helix, 42% strand | F4MEU3 |
Ligands and binding sites
- GOL · Glycerol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 517 | 0.64 | 0.76 | 47 | empty |
| 2 | 77 | 0.39 | 0.78 | 18 | empty |
| 3 | 65 | 0.39 | 0.79 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 315 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 5WOP · High Resolution Structure of Mutant CA09-PB2cap · 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 F4MEU3
- Elsewhere: RCSB PDB 5WOP · PDBe 5WOP · UniProt F4MEU3
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