Q8WX92: Negative elongation factor B (NELFB)

Negative elongation factor B (NELFB) is a 580-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8WX92.

Gene
NELFB
Organism
Homo sapiens
Length
580 residues
Mean pLDDT
89.2
Model
AF-Q8WX92-F1 v6
Model created
1 Aug 2025
PDB structures
14

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Model confidence (pLDDT)

The mean pLDDT of this model is 89.2 (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 accurate72%
70 to 90Confident: backbone generally right22%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions5%

What pLDDT means and how to read it

Function

Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II (PubMed:12612062). The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex (PubMed:10199401). May be able to induce chromatin unfolding (PubMed:11739404). Essential for early embryogenesis; plays an important role in maintaining the undifferentiated state of embryonic stem cells (ESCs) by preventing unscheduled expression of developmental genes (By similarity). Plays a key role in establishing the responsiveness of stem cells to developmental cues; facilitates…

Subunit structure

The NELF complex is composed of NELFA, NELFB, NELFCD (isoform NELF-C or isoform NELF-D) and NELFE; the N-terminus of NELFB binds to the NELFA:NELFCD subcomplex (PubMed:12612062). Binds RNA which may help to stabilize the NELF complex on nucleic acid (PubMed:27282391). Interacts with the first BRCT repeat of BRCA1 (PubMed:11739404). Interacts with KIAA1191 (PubMed:21153684). Interacts with NELFE…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8UHGEM2.7 ÅV=1-554
8UI0EM2.7 ÅV=1-554
8JJ6X-ray2.72 ÅA/B=1-560
8UHDEM2.8 ÅV=1-580
6GMLEM3.2 ÅV=42-580
9J0OEM3.3 ÅV=1-580
9J0PEM3.3 ÅV=1-580
9J0NEM3.4 ÅV=1-580
8UHAEM3.5 ÅV=1-580
7PKSEM3.6 ÅV=1-580
8W8EEM3.9 ÅV=1-580
8RBXEM4.1 Åv=1-580
7YCXEM4.18 Åf=1-580
9VD9EM4.6 Åf=1-580

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