Research workbench
Crystal structure of the complex of hyaluranidase trimer with ascorbic acid at 3.1 a resolution reveals the locations of three binding sites
Analyse Crystal structure of the complex of hyaluranidase trimer with ascorbic acid at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EKA
- Type
- protein
- Length
- 332 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hyaluronidase, phage associated
- EC
- 4.2.2.1
- UniProt
- Q9A0M7
- Ligands
- ASC
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hyaluronidase, phage associated (EC 4.2.2.1) | protein | 332 | 13% helix, 8% strand | Q9A0M7 |
Ligands and binding sites
- ASC · Ascorbic acid · ligand · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3EKA · Crystal structure of the complex of hyaluranidase trimer with ascorbic acid at 3.1 A… · 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 Q9A0M7
- Elsewhere: RCSB PDB 3EKA · PDBe 3EKA · UniProt Q9A0M7
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