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Structure and activity of the GH20 beta-N- acetylhexosaminidase from streptomyces coelicolor A3(2)
Analyse Structure and activity of the GH20 beta-N- acetylhexosaminidase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4C7D
- Type
- protein
- Length
- 987 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-N-acetylhexosaminidase
- EC
- 3.2.1.52
- UniProt
- Q9L068
- Pockets
- 12 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-N-acetylhexosaminidase (EC 3.2.1.52) | protein | 493 | 36% helix, 19% strand | Q9L068 |
| B | Beta-N-acetylhexosaminidase (EC 3.2.1.52) | protein | 494 | 35% helix, 18% strand | Q9L068 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 22 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 210 | 0.55 | 0.79 | 32 | EDO |
| 2 | 234 | 0.55 | 0.78 | 32 | EDO |
| 3 | 105 | 0.54 | 0.84 | 22 | empty |
| 4 | 116 | 0.40 | 0.75 | 22 | empty |
| 5 | 124 | 0.40 | 0.75 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 536 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4C7D · Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces… · 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 Q9L068
- Elsewhere: RCSB PDB 4C7D · PDBe 4C7D · UniProt Q9L068
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