GL1X · GenesisL1 explorer

Research workbench

Crystal structures of cusc review conformational changes accompanying folding and transmembrane channel formation

Analyse Crystal structures of cusc review conformational changes accompanying folding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4K7R
Type
protein
Length
429 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cation efflux system protein cusc
UniProt
P77211
Ligands
3PK
Pockets
3 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 65% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACation efflux system protein cuscprotein42965% helix, 12% strandP77211

Ligands and binding sites

  • 3PK · (2S)-1-(pentanoyloxy)propan-2-yl hexanoate · ligand · chains A

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11220.480.7923empty
2690.330.7618empty
3580.270.7315empty

Compared structures

  • 4K7R · Crystal structures of CusC review conformational changes accompanying folding and… · the same entry in another collection · chain A against A, TM-score 1.00
  • P77211 · AlphaFold monomer V2.0 prediction for cation efflux system protein cusc (P77211) · a predicted model of the same protein · chain A against A, TM-score 0.96

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.