P54132: RecQ-like DNA helicase BLM (BLM)

RecQ-like DNA helicase BLM (BLM) is a 1417-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P54132.

Gene
BLM
Organism
Homo sapiens
Length
1417 residues
Mean pLDDT
60.5
Model
AF-P54132-F1 v6
Model created
1 Aug 2025
PDB structures
15

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Model confidence (pLDDT)

The mean pLDDT of this model is 60.5 (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 accurate30%
70 to 90Confident: backbone generally right17%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions51%

What pLDDT means and how to read it

Function

ATP-dependent DNA helicase that unwinds double-stranded (ds)DNA in a 3'-5' direction (PubMed:24816114, PubMed:25901030, PubMed:9388193, PubMed:9765292). Participates in DNA replication and repair (PubMed:12019152, PubMed:21325134, PubMed:23509288, PubMed:34606619). Involved in 5'-end resection of DNA during double-strand break (DSB) repair: unwinds DNA and recruits DNA2 which mediates the cleavage of 5'-ssDNA (PubMed:21325134). Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution (PubMed:25901030). Binds single-stranded DNA (ssDNA), forked duplex DNA and Holliday junction DNA (PubMed:20639533, PubMed:24257077, PubMed:25901030). Unwinds G-quadruplex DNA;…

Subunit structure

Monomer (PubMed:28228481). Homodimer (via N-terminus) (PubMed:28228481). Homotetramer (via N-terminus); dimer of dimers (PubMed:28228481). Homohexamer (via N-terminus) (PubMed:28228481). Self-association negatively regulates DNA unwinding amplitude and rate. Oligomeric complexes dissociate into monomer in presence of ATP (PubMed:28228481). Part of the BRCA1-associated genome surveillance complex…

Subcellular location

Nucleus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7XV0X-ray1.5 ÅB=146-165
7AUCX-ray1.53 ÅA=636-1070, A=1202-1298
7XUWX-ray1.8 ÅA=550-570
5LUPX-ray2.03 ÅA/B/C/D/E/F/G/H/I/J/K/L=362-414
5MK5X-ray2.16 ÅA/B/C/D=362-414
4O3MX-ray2.3 ÅA=640-1298
5U6KX-ray2.6 ÅL/M/N/O=297-309
3WE2X-ray2.7 ÅA/B=1068-1209
4CDGX-ray2.79 ÅA/B=636-1298
3WE3X-ray2.9 ÅA/B=1068-1209
7AUDX-ray2.96 ÅA/B/C/D/E/F=636-1070, A/B/C/D/E/F=1202-1298
4CGZX-ray3.2 ÅA=636-1298
2KV2NMRA=1210-1294
2MH9NMRA=1067-1210
2RRDNMRA=1200-1295

More AlphaFold highlights

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