O00522: Krev interaction trapped protein 1 (KRIT1)

Krev interaction trapped protein 1 (KRIT1) is a 736-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O00522.

Gene
KRIT1
Organism
Homo sapiens
Length
736 residues
Mean pLDDT
82.8
Model
AF-O00522-F1 v6
Model created
1 Aug 2025
PDB structures
15

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Model confidence (pLDDT)

The mean pLDDT of this model is 82.8 (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 accurate56%
70 to 90Confident: backbone generally right24%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions13%

What pLDDT means and how to read it

Function

Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity (By similarity). Negative regulator of angiogenesis. Inhibits endothelial proliferation, apoptosis, migration, lumen formation and sprouting angiogenesis in primary endothelial cells. Promotes AKT phosphorylation in a NOTCH-dependent and independent manner, and inhibits ERK1/2 phosphorylation indirectly through activation of the DELTA-NOTCH cascade. Acts in concert with CDH5 to establish and maintain correct endothelial cell polarity and vascular lumen and these effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Required for the localization…

Subunit structure

Interacts with CDH5 (PubMed:20332120). Found in a complex, at least composed of ITGB1BP1, KRIT1 and RAP1A. Interacts (via C-terminus FERM domain) with RAP1A (active GTP-bound form preferentially); the interaction does not induce the opening conformation of KRIT1. Interacts (via FERM domain) with RAP1B. Interacts (via N-terminus NPXY motif) with ITGB1BP1; the interaction induces the opening…

Subcellular location

Cytoplasm, cytoskeleton, Cell membrane, Cell junction

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4HDOX-ray1.67 ÅA=417-736
4JIFX-ray1.7 ÅB=170-198
6OQ4X-ray1.75 ÅA=417-736
6OQ3X-ray1.85 ÅA=417-736
6UZKX-ray1.92 ÅA=417-736
4DXAX-ray1.95 ÅB=420-736
4HDQX-ray1.95 ÅA=417-736
8SU8X-ray2.01 ÅA=419-736
8T09X-ray2.15 ÅA=419-736
8T7VX-ray2.25 ÅA=417-736
3U7DX-ray2.49 ÅA/C=417-736
4DX8X-ray2.54 ÅH/I/J/K=1-198
5D68X-ray2.91 ÅA/B/C=259-736
4TKNX-ray3.0 ÅD/E/F=225-237
9PVGX-ray3.0 ÅE/F=227-255

More AlphaFold highlights

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