Research workbench
Apo crystal structure of the colanidase tailspike protein GP150 of phage PHI92
Analyse Apo crystal structure of the colanidase tailspike protein GP150 of phage PHI92 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6E0V
- Type
- protein
- Length
- 1,806 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bacteriophage PHI92 GP150
- UniProt
- I7I026
- Ligands
- SR, CL
- Pockets
- 8 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Bacteriophage PHI92 GP150 | protein | 602 | 6% helix, 48% strand | I7I026 |
Ligands and binding sites
- SR · Strontium ion · metal · 24 copies · chains A, B, C
- CL · Chloride ion · ion · 9 copies · chains A, B, C
- GOL · Glycerol · additive · 8 copies · chains A, C, B
- EDO · 1,2-ethanediol · additive · 8 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 660 | 0.66 | 0.75 | 72 | CL, GOL |
| 2 | 439 | 0.59 | 0.75 | 48 | GOL |
| 3 | 364 | 0.57 | 0.76 | 39 | empty |
| 4 | 341 | 0.57 | 0.76 | 42 | EDO |
| 5 | 63 | 0.46 | 0.84 | 25 | empty |
Interfaces
2 interfaces between chains.
- A–B · 460 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 140 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6E0V · Apo crystal structure of the colanidase tailspike protein gp150 of Phage Phi92 · 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 I7I026
- Elsewhere: RCSB PDB 6E0V · PDBe 6E0V · UniProt I7I026
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