GL1X · GenesisL1 explorer

Research workbench

Crystal structure of the C-terminal part of rhie from burkholderia rhizoxinica

Analyse Crystal structure of the C-terminal part of rhie from burkholderia rhizoxinica in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4KC5
Type
protein
Length
3,632 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Rhie protein
UniProt
A1KQS1
Pockets
20 · best druggability 0.87

Structure

x-ray diffraction · 4 distinct chains · 31% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARhie proteinprotein91431% helix, 25% strandA1KQS1
BRhie proteinprotein90731% helix, 25% strandA1KQS1
CRhie proteinprotein90131% helix, 25% strandA1KQS1
DRhie proteinprotein91031% helix, 26% strandA1KQS1

Ligands and binding sites

  • GOL · Glycerol · additive · chains A

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19590.870.88136empty
210610.860.87125empty
310540.790.8189empty
49790.780.8094empty
5930.770.9720empty

Interfaces

5 interfaces between chains.

  • A–B · 3285 Ų buried · 42 hydrogen bonds · protein-protein
  • C–D · 3239 Ų buried · 40 hydrogen bonds · protein-protein
  • A–D · 752 Ų buried · 11 hydrogen bonds · protein-protein
  • A–C · 178 Ų buried · 1 hydrogen bond · protein-protein
  • B–D · 35 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 4KC5 · Crystal structure of the C-terminal part of RhiE from Burkholderia rhizoxinica · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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