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Crystal structure of SHP/EID1

Analyse Crystal structure of SHP/EID1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4NUF
Type
protein
Length
565 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Maltose ABC transporter periplasmic protein, nuclear receptor subfamily 0 group B member…
UniProt
K0BGG6, Q62227
Ligands
GLC
Pockets
4 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 54% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMaltose ABC transporter periplasmic protein, nuclear receptor subfamily 0 group B member 2 chimeric constructprotein54954% helix, 14% strandK0BGG6, Q62227
PEID1 peptideprotein1675% helix, 0% strand—

Ligands and binding sites

  • GLC · alpha-D-glucopyranose · sugar · 2 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, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13560.710.8338GLC
21210.600.8627empty
33120.570.7736empty
42090.460.7430empty

Interfaces

1 interface between chains.

  • A–P · 855 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 4NUF · Crystal Structure of SHP/EID1 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q62227 · AlphaFold monomer V2.0 prediction for nuclear receptor subfamily 0 group B member 2… · a predicted model of the same protein · chain A against A, TM-score 0.35

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