Research workbench
CPGH89CBM32-6 produced by clostridium perfringens
Analyse CPGH89CBM32-6 produced by clostridium perfringens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4A42
- Type
- protein
- Length
- 253 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-N-acetylglucosaminidase family protein
- EC
- 3.2.1.50
- UniProt
- Q0TST1
- Ligands
- CA
- Pockets
- 2 · best druggability 0.38
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-N-acetylglucosaminidase family protein (EC 3.2.1.50) | protein | 127 | 9% helix, 46% strand | Q0TST1 |
| B | Alpha-N-acetylglucosaminidase family protein (EC 3.2.1.50) | protein | 126 | 9% helix, 52% strand | Q0TST1 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 160 | 0.38 | 0.73 | 31 | empty |
| 2 | 107 | 0.34 | 0.73 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 356 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 4A42 · CpGH89CBM32-6 produced by Clostridium perfringens · 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 Q0TST1
- Elsewhere: RCSB PDB 4A42 · PDBe 4A42 · UniProt Q0TST1
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