Research workbench
Mutated mouse P38 MAP kinase domain in complex with inhibitor pg- 892579
Analyse Mutated mouse P38 MAP kinase domain in complex with inhibitor pg- 892579 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GTM
- Type
- protein
- Length
- 341 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitogen-activated protein kinase 14
- EC
- 2.7.11.24
- UniProt
- P47811
- Ligands
- LID
- Pockets
- 6 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitogen-activated protein kinase 14 (EC 2.7.11.24) | protein | 341 | 40% helix, 17% strand | P47811 |
Ligands and binding sites
- LID · 8-(2-chlorophenylamino)-2-(2,6-difluorophenylamino)-9-ethyl-9H-purine-1,7-diium · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 593 | 0.78 | 0.84 | 69 | LID |
| 2 | 129 | 0.73 | 0.93 | 20 | empty |
| 3 | 90 | 0.37 | 0.76 | 23 | empty |
| 4 | 96 | 0.37 | 0.75 | 15 | empty |
| 5 | 52 | 0.36 | 0.79 | 12 | empty |
Compared structures
- 2GTM · Mutated Mouse P38 MAP Kinase Domain in complex with Inhibitor PG-892579 · the same entry in another collection · chain A against A, TM-score 1.00
- P47811 · AlphaFold monomer V2.0 prediction for mitogen-activated protein kinase 14 (P47811) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P47811
- Elsewhere: RCSB PDB 2GTM · PDBe 2GTM · UniProt P47811
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