GL1X · GenesisL1 explorer

Research workbench

Structure of ring finger protein 165

Analyse Structure of ring finger protein 165 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5D0I
Type
protein
Length
113 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ring finger protein 165
UniProt
Q6ZSG1
Ligands
ZN, SO4

Structure

x-ray diffraction · 2 distinct chains · 22% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARing finger protein 165protein6224% helix, 24% strandQ6ZSG1
BRing finger protein 165protein5120% helix, 20% strandQ6ZSG1

Ligands and binding sites

  • ZN · Zinc ion · metal · 4 copies · chains A, B
  • SO4 · Sulfate ion · ion · chains A, B

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

Interfaces

1 interface between chains.

  • A–B · 387 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 5D0I · Structure of RING finger protein 165 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q6ZSG1 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RNF165 (Q6ZSG1) · a predicted model of the same protein · chain A against A, TM-score 0.94

Analyse

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