Research workbench
High-resolution structures of adenylate kinase from yeast ligated with inhibitor AP5A, showing the pathway of phosphoryl transfer
Analyse High-resolution structures of adenylate kinase from yeast ligated with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AKY
- Type
- protein
- Length
- 218 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenylate kinase
- EC
- 2.7.4.3
- UniProt
- P07170
- Ligands
- AP5, MG
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenylate kinase (EC 2.7.4.3) | protein | 218 | 50% helix, 17% strand | P07170 |
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 | 426 | 0.82 | 0.90 | 57 | MG, AP5 |
| 2 | 72 | 0.34 | 0.76 | 17 | empty |
Compared structures
- 2AKY · High-resolution structures of adenylate kinase from yeast ligated with inhibitor AP5A… · the same entry in another collection · chain A against A, TM-score 1.00
- P07170 · AlphaFold monomer V2.0 prediction for adenylate kinase (P07170) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P07170
- Elsewhere: RCSB PDB 2AKY · PDBe 2AKY · UniProt P07170
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.