Research workbench
Crystal structures of non-phosphorylated MAP2K4
Analyse Crystal structures of non-phosphorylated MAP2K4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VUT
- Type
- protein
- Length
- 463 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual specificity mitogen-activated protein kinase kinase 4
- EC
- 2.7.12.2
- UniProt
- P45985
- Pockets
- 10 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity mitogen-activated protein kinase kinase 4 (EC 2.7.12.2) | protein | 203 | 39% helix, 4% strand | P45985 |
| B | Dual specificity mitogen-activated protein kinase kinase 4 (EC 2.7.12.2) | protein | 260 | 27% helix, 12% strand | P45985 |
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 88 | 0.64 | 0.90 | 24 | empty |
| 2 | 532 | 0.63 | 0.75 | 40 | empty |
| 3 | 321 | 0.60 | 0.78 | 59 | empty |
| 4 | 413 | 0.57 | 0.74 | 57 | empty |
| 5 | 150 | 0.57 | 0.82 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 137 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 3VUT · Crystal structures of non-phosphorylated MAP2K4 · the same entry in another collection · chain A against A, TM-score 1.00
- P45985 · 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 0.93
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 P45985
- Elsewhere: RCSB PDB 3VUT · PDBe 3VUT · UniProt P45985
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