Research workbench
Structure of the LIMK1-atpgammas-CFL1 complex
Analyse Structure of the LIMK1-atpgammas-CFL1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5L6W
- Type
- protein
- Length
- 455 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P53667, P23528
- Ligands
- AGS
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | — | protein | 290 | — | P53667 |
| C | — | protein | 165 | — | P23528 |
Ligands and binding sites
- AGS · Phosphothiophosphoric acid-adenylate ester · ligand · chains L, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5L6W · Structure Of the LIMK1-ATPgammaS-CFL1 Complex · the same entry in another collection · chain L against L, TM-score 1.00
- P53667 · AlphaFold monomer V2.0 prediction for lim domain kinase 1 (P53667) · a predicted model of the same protein · chain L against A, TM-score 0.98
- P23528 · AlphaFold monomer V2.0 prediction for cofilin-1 (P23528) · a predicted model of the same protein · chain C 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 P53667
- Every structure of UniProt P23528
- Elsewhere: RCSB PDB 5L6W · PDBe 5L6W · UniProt P53667 · UniProt P23528
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