Research workbench
Crystal structure of ERK2 complexed with allosteric and ATP- competitive inhibitors.
Analyse Crystal structure of ERK2 complexed with allosteric and ATP- competitive… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AX3
- Type
- protein
- Length
- 341 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitogen-activated protein kinase 1; Allosteric and ATP-competitive inhibitor
- EC
- 2.7.11.24
- UniProt
- P28482
- Ligands
- 5ID
- Pockets
- 4 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitogen-activated protein kinase 1 (EC 2.7.11.24) | protein | 329 | 32% helix, 15% strand | P28482 |
| B | Allosteric and ATP-competitive inhibitor | protein | 12 | 0% helix, 0% strand | — |
Ligands and binding sites
- 5ID · (2R,3R,4S,5R)-2-(4-amino-5-iodo-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-(hydroxymethyl)tetrahydrofuran-3, 4-diol · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 352 | 0.68 | 0.81 | 39 | 5ID |
| 2 | 98 | 0.57 | 0.86 | 22 | empty |
| 3 | 152 | 0.53 | 0.80 | 23 | empty |
| 4 | 84 | 0.33 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 610 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 5AX3 · Crystal structure of ERK2 complexed with allosteric and ATP-competitive inhibitors. · the same entry in another collection · chain A against A, TM-score 1.00
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 P28482
- Elsewhere: RCSB PDB 5AX3 · PDBe 5AX3 · UniProt P28482
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