P07204: Thrombomodulin (THBD)

Thrombomodulin (THBD) is a 575-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P07204.

Gene
THBD
Organism
Homo sapiens
Length
575 residues
Mean pLDDT
78.6
Model
AF-P07204-F1 v6
Model created
1 Aug 2025
PDB structures
13

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Model confidence (pLDDT)

The mean pLDDT of this model is 78.6 (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 accurate41%
70 to 90Confident: backbone generally right35%
50 to 70Low: treat with caution11%
Below 50Very low: often disordered regions13%

What pLDDT means and how to read it

Function

Endothelial cell receptor that plays a critical role in regulating several physiological processes including hemostasis, coagulation, fibrinolysis, inflammation, and angiogenesis (PubMed:10761923). Acts as a cofactor for thrombin activation of protein C/PROC on the surface of vascular endothelial cells leading to initiation of the activated protein C anticoagulant pathway (PubMed:29323190, PubMed:33836597, PubMed:9395524). Also accelerates the activation of the plasma carboxypeptidase B2/CPB2, which catalyzes removal of C-terminal basic amino acids from its substrates including kinins or anaphylatoxins leading to fibrinolysis inhibition (PubMed:26663133). Plays critical protective roles in…

Subunit structure

Interacts with ITGAL, ITGAM and ITGB2. Interacts with thrombin/F2; this interaction switches the specificity of thrombin from a procoagulant to an anticoagulant and antifibrinolytic protease (PubMed:10761923). Interacts with ANGP1 and ANGP2; these interactions significantly inhibit the generation of activated PC and TAFIa/CPB2 by the thrombin/thrombomodulin complex (PubMed:29323190). Interacts…

Subcellular location

Membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1DX5X-ray2.3 ÅI/J/K/L=363-480
5TO3X-ray2.34 ÅB=363-483
3GISX-ray2.4 ÅX/Y/Z=363-483
1HLTX-ray3.0 ÅR=426-444
7T4REM3.3 ÅA=1-516
1ADXNMRA=405-444
1DQBNMRA=362-444
1EGTNMRA=427-444
1FGDNMRA=427-444
1FGENMRA=425-444
1TMRNMRA=389-407
1ZAQNMRA=364-407
2ADXNMRA=405-444

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