GL1X · GenesisL1 explorer

Research workbench

3.5 a cryo-EM structure of human uromodulin filament core

Analyse 3.5 a cryo-EM structure of human uromodulin filament core in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6ZS5
Type
protein
Length
257 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Uromodulin
UniProt
P07911
Ligands
NAG, MAN, BMA
Pockets
2 · best druggability 0.44

Structure

electron microscopy · 2 distinct chains · 0% helix, 45% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUromodulinprotein1160% helix, 49% strandP07911
DUromodulinprotein1410% helix, 41% strandP07911

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, D
  • MAN · alpha-D-mannopyranose · sugar · 2 copies · chains D
  • BMA · beta-D-mannopyranose · sugar

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1790.440.8021empty
21000.400.7724empty

Interfaces

1 interface between chains.

  • A–D · 2069 Ų buried · 29 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

  • 6ZS5 · 3.5 A cryo-EM structure of human uromodulin filament core · the same entry in another collection · chain A against A, TM-score 1.00
  • P07911 · AlphaFold monomer V2.0 prediction for uromodulin (P07911) · a predicted model of the same protein · chain D against A, TM-score 0.88

Analyse

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