Research workbench
CPGH89CBM32-5, from clostridium perfringens, in complex with N- acetylgalactosamine
Analyse CPGH89CBM32-5, from clostridium perfringens, in complex with N… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AAX
- Type
- protein
- Length
- 140 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-N-acetylglucosaminidase
- EC
- 3.2.1.50
- UniProt
- Q8XM24
- Ligands
- NGA, CA, NA
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-N-acetylglucosaminidase (EC 3.2.1.50) | protein | 140 | 8% helix, 50% strand | Q8XM24 |
Ligands and binding sites
- NGA · 2-acetamido-2-deoxy-beta-D-galactopyranose · sugar · chains A
- CA · Calcium ion · metal · chains A
- NA · Sodium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4AAX · CpGH89CBM32-5, from Clostridium perfringens, in complex with N- acetylgalactosamine · 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 Q8XM24
- Elsewhere: RCSB PDB 4AAX · PDBe 4AAX · UniProt Q8XM24
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