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Crystal structure of red abalone verl repeat 1 at 1.8 a resolution

Analyse Crystal structure of red abalone verl repeat 1 at 1.8 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5II5
Type
protein
Length
476 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Maltose-binding periplasmic PROTEIN,VITELLINE envelope sperm lysin receptor
UniProt
P0AEX9, Q8WR62
Ligands
GLC
Pockets
4 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMaltose-binding periplasmic PROTEIN,VITELLINE envelope sperm lysin receptorprotein47635% helix, 28% strandP0AEX9, Q8WR62

Ligands and binding sites

  • GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A
  • PGE · Triethylene glycol · additive · 4 copies · chains A

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

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13080.720.8537GLC
22780.610.7929PGE
32300.560.7836empty
41930.510.7725empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 5II5 · Crystal structure of red abalone VERL repeat 1 at 1.8 A resolution · the same entry in another collection · chain A against A, TM-score 1.00

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