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Crystal structure of human saposin D (triclinic)
Analyse Crystal structure of human saposin D (triclinic) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BQQ
- Type
- protein
- Length
- 316 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proactivator polypeptide
- UniProt
- P07602
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · 4 distinct chains · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Proactivator polypeptide | protein | 79 | 72% helix, 0% strand | P07602 |
| A | Proactivator polypeptide | protein | 80 | 69% helix, 0% strand | P07602 |
| B | Proactivator polypeptide | protein | 78 | 73% helix, 0% strand | P07602 |
| D | Proactivator polypeptide | protein | 79 | 72% helix, 0% strand | P07602 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 187 | 0.52 | 0.78 | 24 | empty |
| 2 | 72 | 0.30 | 0.73 | 16 | empty |
Interfaces
4 interfaces between chains.
- C–D · 488 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 486 Ų buried · 5 hydrogen bonds · protein-protein
- C–A · 407 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 51 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 12 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 3BQQ · PDBe 3BQQ · UniProt P07602
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