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Crystal structure of human soul protein (hexagonal form)
Analyse Crystal structure of human soul protein (hexagonal form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3R8K
- Type
- protein
- Length
- 706 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heme-binding protein 2
- UniProt
- Q9Y5Z4
- Pockets
- 3 · best druggability 0.79
Structure
x-ray diffraction · 3 distinct chains · 21% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Heme-binding protein 2 | protein | 180 | 20% helix, 32% strand | Q9Y5Z4 |
| C | Heme-binding protein 2 | protein | 172 | 22% helix, 35% strand | Q9Y5Z4 |
| D | Heme-binding protein 2 | protein | 174 | 21% helix, 34% strand | Q9Y5Z4 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 467 | 0.79 | 0.87 | 54 | empty |
| 2 | 232 | 0.54 | 0.77 | 29 | empty |
| 3 | 176 | 0.50 | 0.77 | 26 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1334 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 902 Ų buried · 6 hydrogen bonds · protein-protein
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 Q9Y5Z4
- Elsewhere: RCSB PDB 3R8K · PDBe 3R8K · UniProt Q9Y5Z4
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