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Crystal structure of free bglii
Analyse Crystal structure of free bglii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ES8
- Type
- protein
- Length
- 196 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Restriction endonuclease bglii
- EC
- 3.1.21.4
- UniProt
- Q45488
- Pockets
- 3 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Restriction endonuclease bglii (EC 3.1.21.4) | protein | 196 | 31% helix, 37% strand | Q45488 |
Ligands and binding sites
- ACY · Acetic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 129 | 0.53 | 0.81 | 25 | empty |
| 2 | 106 | 0.51 | 0.82 | 23 | empty |
| 3 | 73 | 0.43 | 0.80 | 18 | empty |
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
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 Q45488
- Elsewhere: RCSB PDB 1ES8 · PDBe 1ES8 · UniProt Q45488
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