Research workbench
Crystal structure of the protein-kinase a catalytic subunit from criteculus griseus in complex with compounds RKP191 and RKP190
Analyse Crystal structure of the protein-kinase a catalytic subunit from criteculus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OUC
- Type
- protein
- Length
- 371 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P25321
- Ligands
- AO8, RIP, CL
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 353 | — | P25321 |
| E | — | protein | 18 | — | — |
Ligands and binding sites
- AO8 · [2-[[2-(isoquinolin-5-ylsulfonylamino) ethylamino]methyl]phenyl]boronic acid · ligand · chains A, E
- RIP · beta-D-ribopyranose · ligand · chains A, E
- CL · Chloride ion · ion · chains E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 P25321
- Elsewhere: RCSB PDB 5OUC · PDBe 5OUC · UniProt P25321
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