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Introduction

Protein: cHuman Coagulation factor V, 1czv ^[1]

spinqualitylabelsall models PDB ID 1czv Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1czv, resolution 2.40Å ()
Related:	1czs, 1czt
Structural annotation: Resources: CATH : 1Czva00, 1Czvb00 InterPro : Ipr008972, Ipr002355, Ipr011707, Ipr000421, Ipr008979, Ipr009271, Ipr014693 Pfam : PF00754 SCOP : d1czva_, d1czvb_ UniProt : P12259
Functional annotation: Cellular component: extracellular region Biological process: blood coagulation cell adhesion Molecular function: copper ion binding calcium ion binding metal ion binding oxidoreductase activity
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

Contents 1 Introduction 1.1 Structure 1.2 Function 1.3 Interactions 2 References

Structure

The structure of Human Coagulation Factor V (FV) is sculpted from, originates from, precursors from a polypeptide to a A1-A2-B-A3-C1-C2 layout which results in the activated (FVa) protein.
-Heavy A1-A2 Chain
-Light A3-C1-C2 Chain
FVa consists of a conserved β-Barrel framework acting as a scaffold for three loops and a C2 domain (FVa-C2).
The FVa-C2, which is classified as a distorted jelly-roll β-barrel motif, is compossed of eight major antiparallel strands arranged into two β-sheets of five and three strands packed against one another.
The overall Barrel structure is closed at the top and bottom by three and two straight segments, giving it an overall spherical shape with a flattened upper surface.

Which once activated, enhances the ability of factor Xa to generate α-thrombin from prothrombin (5-Fold).

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Function

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Interactions

References

1. ↑ 10586886