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Crystal structure of human saposin B
Analyse Crystal structure of human saposin B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1N69
- Type
- protein
- Length
- 236 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Saposin B
- UniProt
- P07602
- Ligands
- 3PE
- Pockets
- 3 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Saposin B | protein | 78 | 79% helix, 0% strand | P07602 |
| B | Saposin B | protein | 80 | 75% helix, 0% strand | P07602 |
Ligands and binding sites
- 3PE · 1,2-diacyl-sn-glycero-3-phosphoethanolamine · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1163 | 0.85 | 0.86 | 60 | 3PE |
| 2 | 175 | 0.45 | 0.75 | 26 | empty |
| 3 | 85 | 0.34 | 0.74 | 23 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1338 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 447 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 105 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 9 disulfide (disulfide).
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 P07602
- Elsewhere: RCSB PDB 1N69 · PDBe 1N69 · UniProt P07602
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