Research workbench
Crystal structure of the N-terminal domain of the DNA packaging ATPase from bacteriophage PHI29
Analyse Crystal structure of the N-terminal domain of the DNA packaging ATPase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HD9
- Type
- protein
- Length
- 194 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Encapsidation protein
- UniProt
- P11014
- Pockets
- 2 · best druggability 0.29
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Encapsidation protein | protein | 194 | 31% helix, 23% strand | P11014 |
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 | 59 | 0.29 | 0.74 | 12 | empty |
| 2 | 69 | 0.29 | 0.73 | 15 | empty |
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 5HD9 · Crystal Structure of the N-terminal domain of the DNA packaging ATPase from bacteriophage… · 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 P11014
- Elsewhere: RCSB PDB 5HD9 · PDBe 5HD9 · UniProt P11014
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