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Crystal structure of the factor XA/NAP5 complex

Analyse Crystal structure of the factor XA/NAP5 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2P3F
Type
protein
Length
360 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Coagulation factor X; Anti-coagulant protein 5
EC
3.4.21.6
UniProt
P00742, Q16940
Ligands
NA
Pockets
6 · best druggability 0.51

Structure

x-ray diffraction · 3 distinct chains · 11% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
HCoagulation factor X (EC 3.4.21.6)protein23512% helix, 36% strandP00742
LCoagulation factor X (EC 3.4.21.6)protein510% helix, 27% strandP00742
NAnti-coagulant protein 5protein7414% helix, 22% strandQ16940

Ligands and binding sites

  • NA · Sodium ion · metal · chains H

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11780.510.7829empty
21450.500.7923empty
3770.420.7915empty
4940.390.7622empty
5660.390.7916empty

Interfaces

2 interfaces between chains.

  • H–N · 970 Ų buried · 25 hydrogen bonds · protein-protein
  • H–L · 875 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 13 disulfide (disulfide).

Compared structures

  • 2P3F · Crystal structure of the factor Xa/NAP5 complex · the same entry in another collection · chain H against H, TM-score 1.00
  • P00742 · AlphaFold monomer V2.0 prediction for coagulation factor X (P00742) · a predicted model of the same protein · chain H against A, TM-score 0.98

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