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Crystal structure at 2.9 ångströms resolution of human plasma coagulation factor XI zymogen

Analyse Crystal structure at 2.9 ångströms resolution of human plasma coagulation… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2F83
Type
protein
Length
583 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Coagulation factor XI
EC
3.4.21.27
UniProt
P03951
Ligands
NAG, PT
Pockets
7 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACoagulation factor XI (EC 3.4.21.27)protein58313% helix, 35% strandP03951

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
  • PT · Platinum (II) ion · metal · 2 copies

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

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16830.820.8655empty
24270.680.8033empty
33720.660.8052empty
4690.460.8214empty
51280.440.7617empty

Modifications

Observed in the structure: 16 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

  • P03951 · AlphaFold monomer V2.0 prediction for coagulation factor XI (P03951) · a predicted model of the same protein · chain A against A, TM-score 0.69

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