P53667: LIM domain kinase 1 (LIMK1)

LIM domain kinase 1 (LIMK1) is a 647-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P53667.

Gene
LIMK1
Organism
Homo sapiens
Length
647 residues
Mean pLDDT
75.2
Model
AF-P53667-F1 v6
Model created
1 Aug 2025
PDB structures
10

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Model confidence (pLDDT)

The mean pLDDT of this model is 75.2 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate31%
70 to 90Confident: backbone generally right40%
50 to 70Low: treat with caution11%
Below 50Very low: often disordered regions18%

What pLDDT means and how to read it

Function

Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics. Acts downstream of several Rho family GTPase signal transduction pathways (PubMed:10436159, PubMed:11832213, PubMed:12807904, PubMed:15660133, PubMed:16230460, PubMed:18028908, PubMed:22328514, PubMed:23633677). Activated by upstream kinases including ROCK1, PAK1 and PAK4, which phosphorylate LIMK1 on a threonine residue located in its activation loop (PubMed:10436159). LIMK1 subsequently phosphorylates and inactivates the actin binding/depolymerizing factors cofilin-1/CFL1, cofilin-2/CFL2 and destrin/DSTN, thereby preventing the cleavage of filamentous actin (F-actin), and…

Subunit structure

Interacts (via LIM domain) with the cytoplasmic domain of NRG1. Interacts with NISCH. Interacts with RLIM and RNF6 (By similarity). Self-associates to form homodimers (PubMed:10196227). Interacts with HSP90AA1; this interaction promotes LIMK1 dimerization and subsequent transphosphorylation (PubMed:16641196). Interacts with CDKN1C (PubMed:14530263). Interacts with SSH1 (PubMed:15660133).…

Subcellular location

Cytoplasm, Nucleus, Cytoplasm, cytoskeleton, Cell projection, lamellipodium

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
3S95X-ray1.65 ÅA/B=330-637
8AAUX-ray1.74 ÅL=330-637
6WLYX-ray1.9 ÅB=503-512
5HVJX-ray2.2 ÅA/B=329-638
5NXCX-ray2.25 ÅL=330-637
5L6WX-ray2.53 ÅL=330-637
7ATSX-ray2.8 ÅA=330-637
7ATUX-ray2.8 ÅA/B/C/D=330-637
7B8WX-ray2.8 ÅA/B/C/D=330-637
5HVKX-ray3.5 ÅA/C=329-638

More AlphaFold highlights

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