P00734: Prothrombin (F2)

Prothrombin (F2) is a 622-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P00734.

Gene
F2
Organism
Homo sapiens
Length
622 residues
Mean pLDDT
83.9
Model
AF-P00734-F1 v6
Model created
1 Aug 2025
PDB structures
474

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Model confidence (pLDDT)

The mean pLDDT of this model is 83.9 (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 accurate55%
70 to 90Confident: backbone generally right28%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions10%

What pLDDT means and how to read it

Function

Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing. Activates coagulation factor XI (F11); activation is promoted by the contact with negatively charged surfaces (PubMed:2019570, PubMed:21976677). Triggers the production of pro-inflammatory cytokines, such as MCP-1/CCL2 and IL8/CXCL8, in endothelial cells (PubMed:30568593, PubMed:9780208)

Subunit structure

Heterodimer (named alpha-thrombin) of a light and a heavy chain; disulfide-linked. Forms a heterodimer with SERPINA5. In plasma, interacts (via N-terminus) with alpha-1-microglobulin with molar ratio 1:2 and 1:1; this interaction does not prevent the activation of prothrombin to thrombin. Interacts (thrombin) with iripin-8, a serine protease inhibitor from Ixodes ricinus saliva…

Subcellular location

Secreted, extracellular space

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4UD9X-ray1.12 ÅH=364-622, L=333-360
5AFYX-ray1.12 ÅH=364-621, L=333-361
4UE7X-ray1.13 ÅH=364-621, L=333-360
4UDWX-ray1.16 ÅH=364-621, L=333-360
4UEHX-ray1.16 ÅH=364-621, L=333-361
5AF9X-ray1.18 ÅH=364-621, L=333-361
3RM2X-ray1.23 ÅH=364-622, L=328-363
5AHGX-ray1.24 ÅH=364-621, L=333-361
2BVRX-ray1.25 ÅH=364-622, L=328-363
3VXEX-ray1.25 ÅH=364-622, L=328-363
2UUFX-ray1.26 ÅA=328-363, B=364-622
3SI4X-ray1.27 ÅH=364-622, L=328-363
5JZYX-ray1.27 ÅH=364-622, L=328-363
6FJTX-ray1.27 ÅH=364-621, L=333-360
3U8OX-ray1.28 ÅH=364-622, L=334-363
5MM6X-ray1.29 ÅH=364-622, L=328-363
2CF8X-ray1.3 ÅH=364-620, L=334-361
2CN0X-ray1.3 ÅH=364-620, L=334-361
3SV2X-ray1.3 ÅH=364-622, L=328-363
6TKLX-ray1.3 ÅH=364-622, L=328-363

Showing 20 of 474 experimental structures (best resolution first).

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