P43487: Ran-specific GTPase-activating protein (RANBP1)

Ran-specific GTPase-activating protein (RANBP1) is a 201-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P43487.

Gene
RANBP1
Organism
Homo sapiens
Length
201 residues
Mean pLDDT
83.4
Model
AF-P43487-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 83.4 (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 accurate60%
70 to 90Confident: backbone generally right16%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions14%

What pLDDT means and how to read it

Function

Plays a role in RAN-dependent nucleocytoplasmic transport. Alleviates the TNPO1-dependent inhibition of RAN GTPase activity and mediates the dissociation of RAN from proteins involved in transport into the nucleus (By similarity). Induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins (PubMed:20485264). Promotes the disassembly of the complex formed by RAN and importin beta. Promotes dissociation of RAN from a complex with KPNA2 and CSE1L (By similarity). Required for normal mitotic spindle assembly and normal progress through mitosis via its effect on RAN (PubMed:17671426). Does not increase the RAN…

Subunit structure

Interacts with RAN (via C-terminus of GTP-bound form) but not with GDP-bound RAN (PubMed:7882974, PubMed:7891706, PubMed:8896452). Identified in a complex composed of RAN, RANGAP1 and RANBP1 (PubMed:11832950, PubMed:16428860). Identified in a complex that contains TNPO1, RAN and RANBP1. Identified in a complex that contains CSE1L, KPNA2, RAN and RANBP1 (By similarity). Identified in a complex…

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9N85EM2.6 ÅB=26-168
1K5DX-ray2.7 ÅB/E/H/K=1-201
1K5GX-ray3.1 ÅB/E/H/K=1-201
9YB5EM3.2 ÅC=35-168

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