MolNFT v1 · #47948 · protein
Structure of human hyaluronidase 1, a hyaluronan hydrolyzing enzyme involved in tumor growth and angiogenesis
2PE4 · Hyaluronidase-1: “Structure of human hyaluronidase 1, a hyaluronan hydrolyzing enzyme involved in tumor growth and angiogenesis”. X-ray diffraction, 3 ligands (NAG, MAN, BMA), 4 pockets (best druggability 0.58). MolNFT v1 #47948 on…
- PDB
- 2PE4
- Type
- protein
- Length
- 417 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hyaluronidase-1
- EC
- 3.2.1.35
- UniProt
- Q12794
- Ligands
- NAG, MAN, BMA
- Pockets
- 4 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hyaluronidase-1 (EC 3.2.1.35) | protein | 417 | 41% helix, 15% strand | Q12794 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
- MAN · alpha-D-mannopyranose · sugar · 3 copies
- BMA · beta-D-mannopyranose · sugar
- ACT · Acetate ion · additive · 7 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 217 | 0.58 | 0.79 | 35 | ACT |
| 2 | 111 | 0.48 | 0.80 | 20 | empty |
| 3 | 61 | 0.39 | 0.80 | 15 | empty |
| 4 | 86 | 0.30 | 0.72 | 18 | empty |
Modifications
Observed in the structure: 5 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
- 2PE4 · Structure of Human Hyaluronidase 1, a Hyaluronan Hydrolyzing Enzyme Involved in Tumor… · the same entry in another collection · chain A against A, TM-score 1.00
- Q12794 · AlphaFold monomer V2.0 prediction for hyaluronidase-1 (Q12794) · a predicted model of the same protein · 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 Q12794
- Elsewhere: RCSB PDB 2PE4 · PDBe 2PE4 · UniProt Q12794
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