Research workbench
T4 lysozyme L99A/M102Q with 1-hydro-2-ethyl-1,2-azaborine bound
Analyse T4 lysozyme L99A/M102Q with 1-hydro-2-ethyl-1,2-azaborine bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JWW
- Type
- protein
- Length
- 161 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endolysin
- EC
- 3.2.1.17
- UniProt
- P00720
- Ligands
- 6OQ, CL
- Pockets
- 1 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 65% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endolysin (EC 3.2.1.17) | protein | 161 | 65% helix, 8% strand | P00720 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 219 | 0.52 | 0.77 | 27 | empty |
Compared structures
- 5JWW · T4 Lysozyme L99A/M102Q with 1-Hydro-2-ethyl-1,2-azaborine Bound · 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 P00720
- Elsewhere: RCSB PDB 5JWW · PDBe 5JWW · UniProt P00720
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