O15085: Rho guanine nucleotide exchange factor 11 (ARHGEF11)

Rho guanine nucleotide exchange factor 11 (ARHGEF11) is a 1522-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O15085.

Gene
ARHGEF11
Organism
Homo sapiens
Length
1522 residues
Mean pLDDT
59.6
Model
AF-O15085-F1 v6
Model created
1 Aug 2025
PDB structures
9

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Model confidence (pLDDT)

The mean pLDDT of this model is 59.6 (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 accurate26%
70 to 90Confident: backbone generally right18%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions52%

What pLDDT means and how to read it

Function

May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13. Involved in neurotrophin-induced neurite outgrowth

Subunit structure

Interacts with GNA12 and GNA13 through the RGS domain. Interacts with RHOA, PLXNB1 and PLXNB2. Interacts with SLC1A6 (By similarity). Interacts (via DH domain) with GCSAM (via C-terminus). Found in a complex with ARHGEF11 and ARHGEF12; binding to ARHGEF11 and ARHGEF12 enhances CDC42 GEF activity of PLEKHG4B, and PLEKHG4B, in turn, inhibits ARHGEF11- and ARHGEF12-mediated RHOA activation…

Subcellular location

Cytoplasm, Membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1HTJX-ray2.2 ÅF=281-490
5JHHX-ray2.3 ÅA/E=714-1081
5TYTX-ray2.4 ÅA/B/C/D=40-126
1XCGX-ray2.5 ÅA/E=714-1081
5JHGX-ray2.5 ÅA/E=714-1081
3KZ1X-ray2.7 ÅA/B=710-1085
3T06X-ray2.84 ÅA/E=672-1081
5E6PX-ray3.21 ÅB=42-125
2DLSNMRA=44-123

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