MolNFT v1 · #55921 · protein
Crystal structure of kinase domain of human 5'-AMP-activated protein kinase alpha-2 subunit mutant (T172D)
2YZA · 5'-AMP-activated protein kinase catalytic subunit alpha-2: “Crystal structure of kinase domain of human 5'-AMP-activated protein kinase alpha-2 subunit mutant (T172D)”. X-ray diffraction, 2 pockets (best druggability 0.77). MolNFT…
- PDB
- 2YZA
- Type
- protein
- Length
- 258 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- EC
- 2.7.11.1
- UniProt
- P54646
- Pockets
- 2 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 5'-AMP-activated protein kinase catalytic subunit alpha-2 (EC 2.7.11.1) | protein | 258 | 40% helix, 18% strand | P54646 |
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 | 407 | 0.77 | 0.86 | 46 | empty |
| 2 | 85 | 0.33 | 0.74 | 14 | empty |
Compared structures
- 2YZA · Crystal structure of kinase domain of Human 5'-AMP-activated protein kinase alpha-2… · the same entry in another collection · chain A against A, TM-score 1.00
- P54646 · AlphaFold monomer V2.0 prediction for 5'-AMP-activated protein kinase catalytic subunit… · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P54646
- Elsewhere: RCSB PDB 2YZA · PDBe 2YZA · UniProt P54646
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.