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isolated SBD of BiP with loop34 modification

Analyse isolated SBD of BiP with loop34 modification in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5E86
Type
protein
Length
230 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.681
Source
Homo sapiens
Molecule
78 kDa glucose-regulated protein
UniProt
P11021
Pockets
3 · best druggability 0.56

Structure

x-ray diffraction · resolution 2.681 · 1 distinct chain · 40% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A78 kDa glucose-regulated proteinprotein23040% helix, 25% strandP11021

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11340.560.8224empty
21360.430.7626empty
3770.410.8020empty

Compared structures

  • 5E86 · Isolated sbd of bip with LOOP34 modification · the same entry in another collection · chain A against A, TM-score 1.00
  • P11021 · AlphaFold monomer V2.0 prediction for endoplasmic reticulum chaperone bip (P11021) · a predicted model of the same protein · chain A against A, TM-score 0.46

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