Research workbench
Mycobacterium tuberculosis adenosine kinase bound to 5'-aminoadenosine
Analyse Mycobacterium tuberculosis adenosine kinase bound to 5'-aminoadenosine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6C9Q
- Type
- protein
- Length
- 330 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenosine kinase
- EC
- 2.7.1.20
- UniProt
- A5U4N0
- Ligands
- 5N5
- Pockets
- 3 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenosine kinase (EC 2.7.1.20) | protein | 330 | 43% helix, 22% strand | A5U4N0 |
Ligands and binding sites
- 5N5 · 5'-amino-5'-deoxyadenosine · ligand · 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 | 577 | 0.73 | 0.81 | 63 | 5N5 |
| 2 | 66 | 0.38 | 0.79 | 21 | empty |
| 3 | 52 | 0.36 | 0.79 | 14 | 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 A5U4N0
- Elsewhere: RCSB PDB 6C9Q · PDBe 6C9Q · UniProt A5U4N0
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