Research workbench
Crystal structure of adenosine deaminase complexed with FR235380
Analyse Crystal structure of adenosine deaminase complexed with FR235380 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QXL
- Type
- protein
- Length
- 349 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenosine deaminase
- EC
- 3.5.4.4
- UniProt
- P56658
- Ligands
- FR8, ZN
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenosine deaminase (EC 3.5.4.4) | protein | 349 | 54% helix, 14% strand | P56658 |
Ligands and binding sites
- FR8 · 1-((1R)-1-(hydroxymethyl)-3-{6-[(5-phenylpentanoyl)amino]-1H-indol-1-yl}propyl)-1H-imidazole-4-carboxamide · ligand · chains A
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 388 | 0.74 | 0.84 | 40 | FR8 |
| 2 | 73 | 0.35 | 0.76 | 17 | empty |
| 3 | 57 | 0.25 | 0.72 | 16 | 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 P56658
- Elsewhere: RCSB PDB 1QXL · PDBe 1QXL · UniProt P56658
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