MolNFT v1 · #108159 · protein
Structure of MLK4 kinase domain with atpgammas
4UYA · Mitogen-activated protein kinase kinase kinase MLK4: “Structure of MLK4 kinase domain with atpgammas”. X-ray diffraction, 2 ligands (AGS, MG), 1 pocket (best druggability 0.59). MolNFT v1 #108159 on GenesisL1: 3D structure, binding…
- PDB
- 4UYA
- Type
- protein
- Length
- 274 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitogen-activated protein kinase kinase kinase MLK4
- EC
- 2.7.11.25
- UniProt
- Q5TCX8
- Ligands
- AGS, MG
- Pockets
- 1 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitogen-activated protein kinase kinase kinase MLK4 (EC 2.7.11.25) | protein | 274 | 42% helix, 14% strand | Q5TCX8 |
Ligands and binding sites
- AGS · Phosphothiophosphoric acid-adenylate ester · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 304 | 0.59 | 0.77 | 39 | AGS |
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 Q5TCX8
- Elsewhere: RCSB PDB 4UYA · PDBe 4UYA · UniProt Q5TCX8
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