Research workbench
Three-dimensional structure of beta-acrosin from ram spermatozoa
Analyse Three-dimensional structure of beta-acrosin from ram spermatozoa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FIW
- Type
- protein
- Length
- 274 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-acrosin heavy chain; Beta-acrosin light chain
- UniProt
- Q9GL10
- Ligands
- PBZ, NAG, BMA, MAN, FUL
- Pockets
- 4 · best druggability 0.52
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-acrosin heavy chain | protein | 260 | 11% helix, 37% strand | Q9GL10 |
| L | Beta-acrosin light chain | protein | 14 | 0% helix, 0% strand | — |
Ligands and binding sites
- PBZ · P-amino benzamidine · ligand · 2 copies · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- BMA · beta-D-mannopyranose · sugar
- MAN · alpha-D-mannopyranose · sugar
- FUL · beta-L-fucopyranose · sugar · 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 | 125 | 0.52 | 0.81 | 19 | empty |
| 2 | 51 | 0.41 | 0.83 | 18 | PBZ |
| 3 | 50 | 0.33 | 0.78 | 13 | empty |
| 4 | 53 | 0.27 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–L · 733 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
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 Q9GL10
- Elsewhere: RCSB PDB 1FIW · PDBe 1FIW · UniProt Q9GL10
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