Research workbench
Structure of the human mitogen-activated protein kinase kinase 1 (MEK1)
Analyse Structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3W8Q
- Type
- protein
- Length
- 318 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual specificity mitogen-activated protein kinase kinase 1
- EC
- 2.7.12.2
- UniProt
- Q02750
- Ligands
- AGS
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity mitogen-activated protein kinase kinase 1 (EC 2.7.12.2) | protein | 318 | 46% helix, 14% strand | Q02750 |
Ligands and binding sites
- AGS · Phosphothiophosphoric acid-adenylate ester · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 190 | 0.65 | 0.85 | 30 | AGS |
| 2 | 343 | 0.60 | 0.78 | 43 | empty |
| 3 | 149 | 0.46 | 0.76 | 20 | empty |
| 4 | 97 | 0.42 | 0.78 | 24 | empty |
Compared structures
- 3W8Q · Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (MEK1) · the same entry in another collection · chain A against A, TM-score 1.00
- Q02750 · 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 0.89
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 Q02750
- Elsewhere: RCSB PDB 3W8Q · PDBe 3W8Q · UniProt Q02750
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