MolNFT v1 · #62806 · protein
X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a binary complex with K252A and MG2P
3EQF · Dual specificity mitogen-activated protein kinase kinase 1: “X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a binary complex with K252A…”. X-ray diffraction, 4 ligands (KSA, MG, CA), 2 pockets (best…
- PDB
- 3EQF
- Type
- protein
- Length
- 314 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
- KSA, MG, CA, NA
- Pockets
- 2 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity mitogen-activated protein kinase kinase 1 (EC 2.7.12.2) | protein | 314 | 44% helix, 15% strand | Q02750 |
Ligands and binding sites
- KSA · K-252A · ligand · chains A
- MG · Magnesium ion · metal · chains A
- CA · Calcium ion · metal · chains A
- NA · Sodium 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 587 | 0.75 | 0.82 | 52 | KSA, MG |
| 2 | 383 | 0.65 | 0.79 | 46 | empty |
Compared structures
- 3EQF · X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a binary… · 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 0.98
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 3EQF · PDBe 3EQF · UniProt Q02750
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