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Structure determination of an integral membrane protein at room temperature from crystals in situ

Analyse Structure determination of an integral membrane protein at room temperature… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4YCR
Type
protein
Length
299 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tellurite resistance protein teha homolog
UniProt
P44741
Pockets
7 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 84% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATellurite resistance protein teha homologprotein29984% helix, 0% strandP44741

Ligands and binding sites

  • BOG · octyl beta-D-glucopyranoside · additive · 2 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12250.660.8433empty
22600.620.8139BOG
31090.560.8315empty
4860.410.7711empty
51330.380.7318empty

Compared structures

  • 4YCR · Structure determination of an integral membrane protein at room temperature from crystals… · the same entry in another collection · chain A against A, TM-score 1.00
  • P44741 · AlphaFold monomer V2.0 prediction for tellurite resistance protein teha homolog (P44741) · a predicted model of the same protein · chain A against A, TM-score 1.00

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