Structure of CBM32 from Clostridium perfringens beta-N- acetylhexosaminidase GH84C in complex with galactose. Determined by X-ray diffraction at 1.49 Å resolution. Released 22 Aug 2006.
Explore 2J1A in 3D Show helices and sheets RCSB PDB PDBe
2J1A contains 2 α-helices and 10 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 628-633 | 6 | 1 |
| β-strand | 637 | 1 | 2 |
| β-strand | 643 | 1 | 2 |
| α-helix | 645-648 | 4 | |
| β-strand | 657-658 | 2 | 3 |
| α-helix | 665 | 1 | |
| β-strand | 671-688 | 18 | 1 |
| β-strand | 697-706 | 10 | 1 |
| β-strand | 712-719 | 8 | 1 |
| β-strand | 727-747 | 21 | 1 |
| β-strand | 759-760 | 2 | 3 |
| β-strand | 762-766 | 5 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Hyaluronidase | A | protein | 150 | CLOSTRIDIUM PERFRINGENS | Q0TR53 (AlphaFold model) |
>2J1A_1 HYALURONIDASE (chains A) KGIDPFTNPRTVKITASSEETSGENAPASFASDGDMNTFWHSKWSSPAHEGPHHLTLELD NVYEINKVKYAPRQDSKNGRITGYKVSVSLDGENFTEVKTGTLEDNAAIKFIEFDSVDAK YVRLDVTDSVSDQANGRGKFATAAEVNVHG
The Interaction of a Carbohydrate-Binding Module from a Clostridium Perfringens N-Acetyl-Beta-Hexosaminidase with its Carbohydrate Receptor. Ficko-Blean, E., Boraston, A.B. J Biol Chem (2006) 281:37748. DOI 10.1074/JBC.M606126200 · PubMed
Other PDB entries of the same protein (UniProt Q0TR53 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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