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Structure and mutation analysis of the hexameric P4 from pseudomonas aeruginosa phage phiyy
Analyse Structure and mutation analysis of the hexameric P4 from pseudomonas aeruginosa… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ESV
- Type
- protein
- Length
- 789 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Packaging NTPase
- UniProt
- A0A1U9AK63
- Pockets
- 11 · best druggability 0.71
Structure
x-ray diffraction · 3 distinct chains · 35% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Packaging NTPase | protein | 264 | 35% helix, 20% strand | A0A1U9AK63 |
| A | Packaging NTPase | protein | 258 | 35% helix, 21% strand | A0A1U9AK63 |
| C | Packaging NTPase | protein | 267 | 37% helix, 19% strand | A0A1U9AK63 |
Ligands and binding sites
- TAR · D(-)-tartaric acid · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 560 | 0.71 | 0.80 | 65 | empty |
| 2 | 572 | 0.69 | 0.78 | 74 | empty |
| 3 | 341 | 0.66 | 0.81 | 46 | empty |
| 4 | 295 | 0.64 | 0.81 | 32 | empty |
| 5 | 174 | 0.58 | 0.82 | 33 | TAR |
Interfaces
2 interfaces between chains.
- B–A · 1625 Ų buried · 19 hydrogen bonds · protein-protein
- B–C · 1555 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 7ESV · Structure and mutation analysis of the hexameric P4 from Pseudomonas aeruginosa phage… · the same entry in another collection · chain B against B, 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 A0A1U9AK63
- Elsewhere: RCSB PDB 7ESV · PDBe 7ESV · UniProt A0A1U9AK63
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