MolNFT v1 · #147051 · protein
Apo crystal structure of the colanidase tailspike protein GP150 of phage PHI92
6E0V · Bacteriophage PHI92 GP150: “Apo crystal structure of the colanidase tailspike protein GP150 of phage PHI92”. X-ray diffraction, 2 ligands (SR, CL), 8 pockets (best druggability 0.66). MolNFT v1 #147051 on GenesisL1: 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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