Research workbench
Extremely tight binding of ruthenium complex to glycogen synthase kinase 3
Analyse Extremely tight binding of ruthenium complex to glycogen synthase kinase 3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2JLD
- Type
- protein
- Length
- 706 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P49841
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 349 | — | P49841 |
| B | — | protein | 349 | — | P49841 |
| E | — | protein | 8 | — | — |
Compared structures
- 2JLD · Extremely Tight Binding of Ruthenium Complex to Glycogen Synthase Kinase 3 · the same entry in another collection · chain A against A, TM-score 1.00
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 P49841
- Elsewhere: RCSB PDB 2JLD · PDBe 2JLD · UniProt P49841
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