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Crystal structure of prothrombin deletion mutant residues 146-167 ( form II ).

Analyse Crystal structure of prothrombin deletion mutant residues 146-167 ( form II ). in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5EDK
Type
protein
Length
528 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Prothrombin
EC
3.4.21.5
UniProt
P00734
Ligands
NAG, MG
Pockets
9 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProthrombin (EC 3.4.21.5)protein52814% helix, 19% strandP00734

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
  • MG · Magnesium ion · metal · 4 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11200.620.8620empty
22070.550.7938empty
32460.520.7625empty
42270.500.7528empty
5770.410.7921empty

Modifications

Observed in the structure: 12 disulfide, 10 modified, 3 glycan (disulfide, carboxylation, N-glycosylation).

Compared structures

  • 5EDK · Crystal structure of prothrombin deletion mutant residues 146-167 ( Form II ). · the same entry in another collection · chain A against A, TM-score 1.00

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