Research workbench
Protein kinase a fivefold mutant model of rho-kinase
Analyse Protein kinase a fivefold mutant model of rho-kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GNG
- Type
- protein
- Length
- 361 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Camp-dependent protein kinase, alpha-catalytic subunit; Camp-dependent protein kinase…
- EC
- 2.7.11.11
- UniProt
- P00517, P61926
- Pockets
- 5 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Camp-dependent protein kinase, alpha-catalytic subunit (EC 2.7.11.11) | protein | 341 | 37% helix, 15% strand | P00517 |
| I | Camp-dependent protein kinase inhibitor alpha | protein | 20 | 30% helix, 10% strand | P61926 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 492 | 0.80 | 0.87 | 54 | empty |
| 2 | 107 | 0.53 | 0.82 | 17 | empty |
| 3 | 84 | 0.35 | 0.75 | 16 | empty |
| 4 | 69 | 0.33 | 0.75 | 12 | empty |
| 5 | 51 | 0.27 | 0.74 | 19 | empty |
Interfaces
1 interface between chains.
- A–I · 1048 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (phosphorylation).
Compared structures
- 2GNG · Protein kinase A fivefold mutant model of Rho-kinase · the same entry in another collection · chain A against A, TM-score 1.00
- P61926 · AlphaFold monomer V2.0 prediction for camp-dependent protein kinase inhibitor alpha… · a predicted model of the same protein · chain I against A, TM-score 0.41
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 P00517
- Every structure of UniProt P61926
- Elsewhere: RCSB PDB 2GNG · PDBe 2GNG · UniProt P00517 · UniProt P61926
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