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Structural and biochemical characterization of FK506 binding domain from Plasmodium vivax
Analyse Structural and biochemical characterization of FK506 binding domain from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KI3
- Type
- protein
- Length
- 126 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- NOT
- Source
- Plasmodium vivax
- Molecule
- 70 kDa peptidylprolyl isomerase, putative
- UniProt
- A5K8X6
- Pockets
- 1 · best druggability 0.38
Structure
solution nmr · resolution NOT · 1 distinct chain · 11% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 70 kDa peptidylprolyl isomerase, putative | protein | 126 | 11% helix, 35% strand | A5K8X6 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.38 | 0.80 | 13 | empty |
Compared structures
- 2KI3 · Structural and biochemical characterization of FK506 binding domain from plasmodium vivax · the same entry in another collection · chain A against A, TM-score 1.00
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 A5K8X6
- Elsewhere: RCSB PDB 2KI3 · PDBe 2KI3 · UniProt A5K8X6
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