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Phosphorylated MAP kinase P38-gamma
Analyse Phosphorylated MAP kinase P38-gamma in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CM8
- Type
- protein
- Length
- 658 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphorylated MAP kinase P38-gamma
- UniProt
- P53778
- Ligands
- ANP, MG
- Pockets
- 8 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Phosphorylated MAP kinase P38-gamma | protein | 329 | 39% helix, 14% strand | P53778 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 333 | 0.62 | 0.78 | 43 | MG, ANP |
| 2 | 191 | 0.61 | 0.82 | 25 | MG, ANP |
| 3 | 153 | 0.44 | 0.75 | 22 | MG |
| 4 | 148 | 0.44 | 0.75 | 29 | empty |
| 5 | 127 | 0.42 | 0.75 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 312 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (phosphorylation).
Compared structures
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 P53778
- Elsewhere: RCSB PDB 1CM8 · PDBe 1CM8 · UniProt P53778
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