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The crystal structure of B204, the DNA-packaging ATPase from sulfolobus turreted icosahedral virus
Analyse The crystal structure of B204, the DNA-packaging ATPase from sulfolobus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4R2H
- Type
- protein
- Length
- 205 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Stiv B204 ATPase
- UniProt
- Q6Q0J1
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Stiv B204 ATPase | protein | 205 | 41% helix, 21% strand | Q6Q0J1 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 123 | 0.44 | 0.78 | 22 | empty |
| 2 | 156 | 0.44 | 0.75 | 19 | empty |
| 3 | 73 | 0.40 | 0.78 | 14 | empty |
Compared structures
- 4R2H · The Crystal Structure of B204, the DNA-packaging ATPase from Sulfolobus Turreted… · 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 Q6Q0J1
- Elsewhere: RCSB PDB 4R2H · PDBe 4R2H · UniProt Q6Q0J1
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