Research workbench
Rifined crystal structure of non-phosphorylated MAP2K6 in a putative auto-inhibition state
Analyse Rifined crystal structure of non-phosphorylated MAP2K6 in a putative… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VN9
- Type
- protein
- Length
- 291 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual specificity mitogen-activated protein kinase kinase 6
- EC
- 2.7.12.2
- UniProt
- P52564
- Ligands
- ANK, MG
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity mitogen-activated protein kinase kinase 6 (EC 2.7.12.2) | protein | 291 | 42% helix, 15% strand | P52564 |
Ligands and binding sites
- ANK · 9-{5-O-[(R)-hydroxy{[(S)-hydroxy(phosphonoamino)phosphoryl]oxy}phosphoryl]-beta-L-ribofuranosyl}-9H-purin-6-amine · ligand · chains A
- MG · Magnesium ion · metal · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 349 | 0.68 | 0.81 | 39 | ANK, MG |
| 2 | 85 | 0.31 | 0.73 | 15 | empty |
Compared structures
- 3VN9 · Rifined Crystal structure of non-phosphorylated MAP2K6 in a putative auto-inhibition state · the same entry in another collection · chain A against A, TM-score 1.00
- P52564 · AlphaFold monomer V2.0 prediction for dual specificity mitogen- activated protein kinase… · 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 P52564
- Elsewhere: RCSB PDB 3VN9 · PDBe 3VN9 · UniProt P52564
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