MolNFT v2 · #15747 · protein
Crystal Structure of Adenosine Deaminase Complexed with FR230513
1NDY: “Crystal Structure of Adenosine Deaminase Complexed with FR230513”. X-ray diffraction at 2, 2 ligands (FR3, ZN), 3 pockets (best druggability 0.73). MolNFT v2 #15747 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1NDY
- Type
- protein
- Length
- 349 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Bos taurus
- Molecule
- Adenosine Deaminase
- EC
- 3.5.4.4
- UniProt
- P56658
- Ligands
- FR3, ZN
- Pockets
- 3 · best druggability 0.73
Structure
x-ray diffraction · resolution 2 · 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
- FR3 · 1-((1R)-1-(hydroxymethyl)-3-(1-naphthyl)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 | 338 | 0.73 | 0.85 | 40 | FR3 |
| 2 | 92 | 0.39 | 0.77 | 19 | empty |
| 3 | 64 | 0.33 | 0.76 | 12 | 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 1NDY · PDBe 1NDY · UniProt P56658
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