Q96QB1: Rho GTPase-activating protein 7 (DLC1)

Rho GTPase-activating protein 7 (DLC1) is a 1528-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96QB1.

Gene
DLC1
Organism
Homo sapiens
Length
1528 residues
Mean pLDDT
55.9
Model
AF-Q96QB1-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 55.9 (low 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 accurate20%
70 to 90Confident: backbone generally right17%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions57%

What pLDDT means and how to read it

Function

Functions as a GTPase-activating protein for the small GTPases RHOA, RHOB, RHOC and CDC42, terminating their downstream signaling. This induces morphological changes and detachment through cytoskeletal reorganization, playing a critical role in biological processes such as cell migration and proliferation. Also functions in vivo as an activator of the phospholipase PLCD1. Active DLC1 increases cell migration velocity but reduces directionality. Required for growth factor-induced epithelial cell migration; in resting cells, interacts with TNS3 while PTEN interacts with the p85 regulatory subunit of the PI3K kinase complex but growth factor stimulation induces phosphorylation of TNS3 and…

Subunit structure

Interacts with EF1A1, facilitates EF1A1 distribution to the membrane periphery and ruffles upon growth factor stimulation and suppresses cell migration (PubMed:19158340). Interacts with tensin TNS1 (via N-terminus); the interaction is decreased by phosphorylation of TNS1 (PubMed:19826001, PubMed:20798394, PubMed:26427649). Interacts with TNS3 and PTEN; in resting cells, interacts with TNS3 (via…

Subcellular location

Cytoplasm, Cell junction, focal adhesion, Membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5FZTX-ray2.1 ÅB=904-926
3KUQX-ray2.3 ÅA=1074-1283
7TPBX-ray3.2 ÅB/D/F/H=1074-1283
2DKYNMRA=449-515
2GYTNMRA=449-513
2KAPNMRA=454-513
2LOZNMRB=811-824

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