MolNFT v1 · #185623 · protein
Endolysin from bacteriophage ENC34, catalytic domain
7Q47: “Endolysin from bacteriophage ENC34, catalytic domain”. X-ray diffraction, 2 ligands (NA, CL), 3 pockets (best druggability 0.49). MolNFT v1 #185623 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7Q47
- Type
- protein
- Length
- 324 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endolysin
- UniProt
- H6WYJ5
- Ligands
- NA, CL
- Pockets
- 3 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endolysin | protein | 166 | 43% helix, 4% strand | H6WYJ5 |
| B | Endolysin | protein | 158 | 46% helix, 4% strand | H6WYJ5 |
Ligands and binding sites
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 | 183 | 0.49 | 0.77 | 20 | empty |
| 2 | 75 | 0.30 | 0.73 | 15 | empty |
| 3 | 51 | 0.24 | 0.72 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 250 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 7Q47 · Endolysin from bacteriophage Enc34, catalytic domain · 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 H6WYJ5
- Elsewhere: RCSB PDB 7Q47 · PDBe 7Q47 · UniProt H6WYJ5
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