Research workbench
Crystal structure of unsaturated glucuronyl hydrolase specific for heparin
Analyse Crystal structure of unsaturated glucuronyl hydrolase specific for heparin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WIW
- Type
- protein
- Length
- 371 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycosyl hydrolase family 88
- UniProt
- C6Y1N7
- Pockets
- 2 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycosyl hydrolase family 88 | protein | 371 | 54% helix, 13% strand | C6Y1N7 |
Ligands and binding sites
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 119 | 0.53 | 0.82 | 25 | empty |
| 2 | 169 | 0.52 | 0.78 | 28 | EPE |
Compared structures
- 3WIW · Crystal structure of unsaturated glucuronyl hydrolase specific for heparin · 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 C6Y1N7
- Elsewhere: RCSB PDB 3WIW · PDBe 3WIW · UniProt C6Y1N7
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