P00735: Prothrombin (F2)

Prothrombin (F2) is a 625-residue protein from Bos taurus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P00735.

Gene
F2
Organism
Bos taurus
Length
625 residues
Mean pLDDT
83.6
Model
AF-P00735-F1 v6
Model created
1 Aug 2025
PDB structures
31

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Model confidence (pLDDT)

The mean pLDDT of this model is 83.6 (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 accurate56%
70 to 90Confident: backbone generally right24%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions9%

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 (By similarity). Activates coagulation factor XI (F11); activation is promoted by the contact with negatively charged surfaces (By similarity). Triggers the production of pro-inflammatory cytokines, such as MCP-1/CCL2 and IL8/CXCL8, in endothelial cells (By similarity)

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; this interaction does not prevent the activation of prothrombin to thrombin

Subcellular location

Secreted, extracellular space

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7A0DX-ray1.6 ÅHHH=367-625, LLL=318-366
1NL1X-ray1.9 ÅA=44-190
7A0EX-ray1.9 ÅHHH=367-625, LLL=318-366
1ETRX-ray2.2 ÅH=367-625, L=318-366
1MKXX-ray2.2 ÅH=367-625, K=318-625, L=318-366
1UCYX-ray2.2 ÅE=517-625, H=367-516, J/L/M=318-366, K/N=367-625
2PF2X-ray2.2 ÅA=44-199
3PMAX-ray2.2 ÅA/C=336-364, B/D=367-625
1BBRX-ray2.3 ÅE=517-625, H=367-515, J/L/M=318-366, K/N=367-625
1ETSX-ray2.3 ÅH=367-625, L=318-366
1MKWX-ray2.3 ÅH=367-625, K=318-625, L=318-366
1NL2X-ray2.3 ÅA=44-189
2ODYX-ray2.35 ÅA/C=318-366, B/D=367-625
1ETTX-ray2.5 ÅH=367-625, L=318-366
1ID5X-ray2.5 ÅH=367-622, L=318-366
1UVTX-ray2.5 ÅH=367-625, L=318-366
1YCPX-ray2.5 ÅH=367-625, J/L=318-366, K=367-516, M=517-625
2SPTX-ray2.5 ÅA=44-188
1AVGX-ray2.6 ÅH=367-625, L=326-366
1TBRX-ray2.6 ÅH/K=367-625, J/L=318-366

Showing 20 of 31 experimental structures (best resolution first).

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