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Crystal structure of apo TrkA
Analyse Crystal structure of apo TrkA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4F0I
- Type
- protein
- Length
- 578 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.302
- Source
- Homo sapiens
- Molecule
- High affinity nerve growth factor receptor
- EC
- 2.7.10.1
- UniProt
- P04629
- Pockets
- 6 · best druggability 0.78
Structure
x-ray diffraction · resolution 2.302 · 2 distinct chains · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | High affinity nerve growth factor receptor (EC 2.7.10.1) | protein | 284 | 41% helix, 17% strand | P04629 |
| B | High affinity nerve growth factor receptor (EC 2.7.10.1) | protein | 294 | 40% helix, 17% strand | P04629 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1191 | 0.78 | 0.79 | 98 | empty |
| 2 | 197 | 0.60 | 0.82 | 24 | empty |
| 3 | 182 | 0.57 | 0.80 | 24 | empty |
| 4 | 163 | 0.50 | 0.78 | 18 | empty |
| 5 | 97 | 0.36 | 0.74 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 604 Ų buried · 7 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 P04629
- Elsewhere: RCSB PDB 4F0I · PDBe 4F0I · UniProt P04629
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