Research workbench
CpGH89CBM32-4 (seleno-methionine labeled) produced by Clostridium perfringens
Analyse CpGH89CBM32-4 (seleno-methionine labeled) 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
- 4A3Z
- Type
- protein
- Length
- 136 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.55
- Source
- CLOSTRIDIUM PERFRINGENS
- Molecule
- Alpha-N-acetylglucosaminidase family protein
- EC
- 3.2.1.50
- UniProt
- Q0TST1
- Ligands
- CA
Structure
x-ray diffraction · resolution 1.55 · 1 distinct chain · 5% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-N-acetylglucosaminidase family protein (EC 3.2.1.50) | protein | 136 | 5% helix, 50% strand | Q0TST1 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 4A3Z · CPGH89CBM32-4 (seleno-methionine labeled) 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 4A3Z · PDBe 4A3Z · UniProt Q0TST1
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