P18754: Regulator of chromosome condensation (RCC1)

Regulator of chromosome condensation (RCC1) is a 421-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P18754.

Gene
RCC1
Organism
Homo sapiens
Length
421 residues
Mean pLDDT
93.8
Model
AF-P18754-F1 v6
Model created
1 Aug 2025
PDB structures
11

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Model confidence (pLDDT)

The mean pLDDT of this model is 93.8 (very high 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 accurate91%
70 to 90Confident: backbone generally right3%
50 to 70Low: treat with caution1%
Below 50Very low: often disordered regions5%

What pLDDT means and how to read it

Function

Guanine-nucleotide releasing factor that promotes the exchange of Ran-bound GDP by GTP, and thereby plays an important role in RAN-mediated functions in nuclear import and mitosis (PubMed:11336674, PubMed:17435751, PubMed:1944575, PubMed:20668449, PubMed:22215983, PubMed:29042532). Contributes to the generation of high levels of chromosome-associated, GTP-bound RAN, which is important for mitotic spindle assembly and normal progress through mitosis (PubMed:12194828, PubMed:17435751, PubMed:22215983). Via its role in maintaining high levels of GTP-bound RAN in the nucleus, contributes to the release of cargo proteins from importins after nuclear import (PubMed:22215983). Involved in the…

Subunit structure

Interacts with RAN (PubMed:11336674, PubMed:17435751, PubMed:18762580, PubMed:29040603). Interacts with KPNA3 (PubMed:34564892). Interacts (via N-terminus and RCC1 repeats) with KPNA4 (PubMed:29042532). Interacts with ARRB2; the interaction is detected in the nucleus upon OR1D2 stimulation (PubMed:16820410)

Subcellular location

Nucleus, Chromosome, Cytoplasm

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6DUBX-ray1.2 ÅE/F=2-7
5E1DX-ray1.45 ÅD/E=3-7
5E1BX-ray1.65 ÅD/E=2-7
1A12X-ray1.7 ÅA/B/C=9-421
5E1MX-ray1.75 ÅD/E=3-7
5E2AX-ray1.75 ÅD/E=2-7
1I2MX-ray1.76 ÅB/D=20-421
5E2BX-ray1.95 ÅD/E=3-7
5E1OX-ray2.0 ÅD/E=3-7
8UX1EM2.5 ÅL=2-421
5TBKX-ray3.45 ÅI/J/K/L/M/N/O/P=1-421

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