Research workbench
Crystal structure of C-AMP dependent kinase (PKA) bound to hydroxyfasudil
Analyse Crystal structure of C-AMP dependent kinase (PKA) bound to hydroxyfasudil in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ERZ
- Type
- protein
- Length
- 356 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P05132, P61926
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | — | protein | 336 | — | P05132 |
| I | — | protein | 20 | — | P61926 |
Compared structures
- 2ERZ · Crystal Structure of c-AMP Dependent Kinase (PKA) bound to hydroxyfasudil · the same entry in another collection · chain E against E, 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 0.40
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 P05132
- Every structure of UniProt P61926
- Elsewhere: RCSB PDB 2ERZ · PDBe 2ERZ · UniProt P05132 · UniProt P61926
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