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Crystal structure of red abalone VERL repeat 3 at 2.9 A resolution

Analyse Crystal structure of red abalone VERL repeat 3 at 2.9 A resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5IIC
Type
protein
Length
939 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.9
Source
Escherichia coli; Haliotis rufescens
Molecule
Maltose-binding periplasmic protein,Vitelline envelope sperm lysin receptor
UniProt
P0AEX9, Q8WR62
Ligands
GLC, NAG
Pockets
7 · best druggability 0.86

Structure

x-ray diffraction · resolution 2.9 · 2 distinct chains · 37% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMaltose-binding periplasmic protein,Vitelline envelope sperm lysin receptorprotein47236% helix, 29% strandP0AEX9, Q8WR62
BMaltose-binding periplasmic protein,Vitelline envelope sperm lysin receptorprotein46737% helix, 28% strandP0AEX9, Q8WR62

Ligands and binding sites

  • GLC · alpha-D-glucopyranose · sugar · 4 copies · chains A, B
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111480.860.87121empty
27120.770.8258GLC, NAG
38000.760.8089empty
42650.730.8626GLC
5880.690.9315empty

Interfaces

1 interface between chains.

  • A–B · 1742 Ų buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide, 4 glycan (disulfide, N-glycosylation).

Compared structures

  • 5IIC · Crystal structure of red abalone verl repeat 3 at 2.9 a resolution · the same entry in another collection · chain A against A, TM-score 1.00

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