Research workbench
Lim domain kinase 2 (LIMK2) in complex with th-300
Analyse Lim domain kinase 2 (LIMK2) in complex with th-300 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NXD
- Type
- protein
- Length
- 542 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P53671
- Ligands
- 9D8
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 271 | — | P53671 |
Ligands and binding sites
- 9D8 · 4-[(3-chlorophenyl)sulfamoyl]-~{N}-(phenylmethyl)-~{N}-propyl-benzamide · ligand · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 P53671
- Elsewhere: RCSB PDB 5NXD · PDBe 5NXD · UniProt P53671
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