Research workbench
Crystal structure of M tuberculosis adenosine kinase complexed with AMP-pcp (non-hydrolyzable ATP analog)
Analyse Crystal structure of M tuberculosis adenosine kinase complexed with AMP-pcp… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PKN
- Type
- protein
- Length
- 323 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenosine kinase
- EC
- 2.7.1.20
- UniProt
- P83734
- Ligands
- ACP
- Pockets
- 2 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenosine kinase (EC 2.7.1.20) | protein | 323 | 42% helix, 21% strand | P83734 |
Ligands and binding sites
- ACP · Phosphomethylphosphonic acid adenylate ester · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 320 | 0.56 | 0.76 | 54 | ACP |
| 2 | 55 | 0.53 | 0.88 | 22 | empty |
Compared structures
- 2PKN · Crystal structure of M tuberculosis Adenosine Kinase complexed with AMP-PCP… · 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 P83734
- Elsewhere: RCSB PDB 2PKN · PDBe 2PKN · UniProt P83734
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