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Crystal structure of human TRAP1 with DN203495
Analyse Crystal structure of human TRAP1 with DN203495 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7C05
- Type
- protein
- Length
- 435 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat shock protein 75 kda, mitochondrial
- UniProt
- Q12931
- Ligands
- FE6
- Pockets
- 8 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heat shock protein 75 kda, mitochondrial | protein | 435 | 39% helix, 24% strand | Q12931 |
Ligands and binding sites
- FE6 · 1-[(4-bromanyl-2-fluoranyl-phenyl)methyl]-4-chloranyl-pyrazolo[3,4-d]pyrimidin-6-amine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 165 | 0.71 | 0.89 | 23 | FE6 |
| 2 | 173 | 0.49 | 0.77 | 20 | empty |
| 3 | 96 | 0.47 | 0.81 | 20 | empty |
| 4 | 104 | 0.39 | 0.76 | 16 | empty |
| 5 | 90 | 0.38 | 0.76 | 15 | empty |
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 Q12931
- Elsewhere: RCSB PDB 7C05 · PDBe 7C05 · UniProt Q12931
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