P43403: Tyrosine-protein kinase ZAP-70 (ZAP70)

Tyrosine-protein kinase ZAP-70 (ZAP70) is a 619-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P43403.

Gene
ZAP70
Organism
Homo sapiens
Length
619 residues
Mean pLDDT
84.9
Model
AF-P43403-F1 v6
Model created
1 Aug 2025
PDB structures
15

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Model confidence (pLDDT)

The mean pLDDT of this model is 84.9 (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 accurate64%
70 to 90Confident: backbone generally right22%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions10%

What pLDDT means and how to read it

Function

Tyrosine kinase that plays an essential role in regulation of the adaptive immune response. Regulates motility, adhesion and cytokine expression of mature T-cells, as well as thymocyte development. Also contributes to the development and activation of primary B-lymphocytes. When antigen presenting cells (APC) activate T-cell receptor (TCR), a serie of phosphorylations lead to the recruitment of ZAP70 to the phosphorylated TCR components CD3E and CD247/CD3Z through ITAM motif at the plasma membrane (PubMed:7509083). This recruitment serves to localization to the stimulated TCR and to relieve its autoinhibited conformation. Release of ZAP70 active conformation is further stabilized by…

Subunit structure

Interacts with CD247/CD3Z; this interaction docks ZAP70 at the stimulated TCR (PubMed:1423621, PubMed:26783323, PubMed:7659156). Interacts with NFAM1 (PubMed:15143214). Interacts with adapter protein SLA; this interaction negatively regulates T-cell receptor signaling (PubMed:10449770). Interacts with FCRL3 (PubMed:12051764, PubMed:19843936). Interacts with VAV1 (PubMed:9151714). Interacts with…

Subcellular location

Cytoplasm, Cell membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7SIYX-ray1.48 ÅZ=292-296
2OQ1X-ray1.9 ÅA=3-256
2Y1NX-ray2.0 ÅB/D=286-297
4XZ0X-ray2.0 ÅA=1-259
2CBLX-ray2.1 ÅB=286-297
3ZNIX-ray2.21 ÅB/F/J/N=286-297
1U59X-ray2.3 ÅA=327-606
5O76X-ray2.47 ÅB/D=286-297
1M61X-ray2.5 ÅA=1-256
2OZOX-ray2.6 ÅA=1-606
4A4CX-ray2.7 ÅB=286-297
4A4BX-ray2.79 ÅB=286-297
4XZ1X-ray2.8 ÅA=1-259
1FBVX-ray2.9 ÅB=289-297
4K2RX-ray3.0 ÅA=1-606

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