Q6XZF7: Dynamin-binding protein (DNMBP)

Dynamin-binding protein (DNMBP) is a 1577-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q6XZF7.

Gene
DNMBP
Organism
Homo sapiens
Length
1577 residues
Mean pLDDT
63.9
Model
AF-Q6XZF7-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 63.9 (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 accurate27%
70 to 90Confident: backbone generally right26%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions41%

What pLDDT means and how to read it

Function

Plays a critical role as a guanine nucleotide exchange factor (GEF) for CDC42 in several intracellular processes associated with the actin and microtubule cytoskeleton. Regulates the structure of apical junctions through F-actin organization in epithelial cells (PubMed:17015620, PubMed:19767742). Participates in the normal lumenogenesis of epithelial cell cysts by regulating spindle orientation (PubMed:20479467). Plays a role in ciliogenesis (By similarity). May play a role in membrane trafficking between the cell surface and the Golgi (By similarity)

Subunit structure

Binds DNM1 via its N-terminal SH3 domains. The C-terminal SH3 domain binds a complex containing actin, tubulin, Hsp70 and actin-regulatory proteins, such as ENAH, EVL, WIRE, CR16, WAVE1 and NAP1L1 (By similarity). Interacts with FASLG (PubMed:19807924). Interacts (via SH3 domain 6) with WASL (PubMed:17015620, PubMed:19767742, PubMed:24332715). Interacts (via SH3 domain 6) interacts with ENAH…

Subcellular location

Cytoplasm, Golgi apparatus, Golgi stack, Cytoplasm, cytoskeleton, Synapse, Cell junction

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4CC2X-ray1.55 ÅA/C=1513-1577
4GLMX-ray1.9 ÅA/B/C/D=246-301
4CC3X-ray1.97 ÅA/C/E/G=1513-1577
4CC7X-ray1.97 ÅA/C/E/G/I/K/M=1513-1577
4CC4X-ray2.6 ÅB/D/F=1513-1577
1UG1NMRA=1278-1355
1UHCNMRA=1510-1575

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