MolNFT v2 · #155650 · protein

Crystal structure of CLK1 in complex with CX-4945

6KHD: “Crystal structure of CLK1 in complex with CX-4945”. X-ray diffraction at 2.7, 1 ligand (3NG). MolNFT v2 #155650 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6KHD
Type: protein
Length: 979 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.7
Source: Homo sapiens
UniProt: P49759
Ligands: 3NG

Structure

x-ray diffraction · resolution 2.7 · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	322	—	P49759
B	—	protein	332	—	P49759
C	—	protein	325	—	P49759

Ligands and binding sites

3NG · 5-[(3-chlorophenyl)amino]benzo[c][2,6]naphthyridine-8-carboxylic acid · ligand · 3 copies · chains A, B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

6KHD · Crystal structure of CLK1 in complex with cx-4945 · the same entry in another collection · chain A against A, TM-score 1.00
P49759 · AlphaFold monomer V2.0 prediction for dual specificity protein kinase CLK1 (P49759) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 P49759
Elsewhere: RCSB PDB 6KHD · PDBe 6KHD · UniProt P49759

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