P0DMV9: Heat shock 70 kDa protein 1B (HSPA1B)

Heat shock 70 kDa protein 1B (HSPA1B) is a 641-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P0DMV9.

Gene
HSPA1B
Organism
Homo sapiens
Length
641 residues
Mean pLDDT
88.7
Model
AF-P0DMV9-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 88.7 (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 accurate69%
70 to 90Confident: backbone generally right23%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions5%

What pLDDT means and how to read it

Function

Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but…

Subunit structure

May be an auxiliary component of the CatSper complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661). Interacts with CHCHD3, DNAJC7, IRAK1BP1, PPP5C and TSC2 (PubMed:12853476, PubMed:15383005, PubMed:15963462, PubMed:17233114, PubMed:18620420, PubMed:21081504). Interacts with TERT; the interaction occurs in the absence of the RNA component,…

Subcellular location

Cytoplasm, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7F4XOther1.6 ÅA=3-380
7F50X-ray1.7 ÅA=3-380
7F4ZX-ray1.8 ÅA=3-380
4J8FX-ray2.7 ÅA=1-382, A=384-600
6FDTNMRB=633-641

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