Research workbench
Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations
Analyse Atomic structure of adenosine deaminase complexed with a transition-state… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ADA
- 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
- P03958
- Ligands
- HPR, ZN
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenosine deaminase (EC 3.5.4.4) | protein | 349 | 51% helix, 14% strand | P03958 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 183 | 0.67 | 0.86 | 30 | HPR |
| 2 | 87 | 0.37 | 0.76 | 16 | empty |
Compared structures
- 2ADA · Atomic structure of adenosine deaminase complexed with a transition-state analog… · the same entry in another collection · chain A against A, TM-score 1.00
- P03958 · AlphaFold monomer V2.0 prediction for adenosine deaminase (P03958) · a predicted model of the same protein · 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 P03958
- Elsewhere: RCSB PDB 2ADA · PDBe 2ADA · UniProt P03958
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