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Crystal structure of Pisum sativum vicilin

Analyse Crystal structure of Pisum sativum vicilin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7U1I
Type
protein
Length
1,081 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
3.1
Source
Pisum sativum
Molecule
Vicilin
UniProt
Q702P1
Pockets
13 · best druggability 0.79

Structure

x-ray diffraction · resolution 3.1 · 3 distinct chains · 18% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AVicilinprotein36218% helix, 42% strandQ702P1
BVicilinprotein36018% helix, 45% strandQ702P1
CVicilinprotein35917% helix, 40% strandQ702P1

Pockets

13 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11170.790.9725empty
21120.790.9824empty
33110.740.8640empty
49770.690.74106empty
52460.640.8230empty

Interfaces

3 interfaces between chains.

  • A–B · 2546 Ų buried · 34 hydrogen bonds · protein-protein
  • B–C · 2516 Ų buried · 36 hydrogen bonds · protein-protein
  • A–C · 2456 Ų buried · 28 hydrogen bonds · protein-protein

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