GL1X · GenesisL1 explorer

Research workbench

Crystal structure of putative CUTA1 from homo sapiens at 2.05A resolution

Analyse Crystal structure of putative CUTA1 from homo sapiens at 2.05A resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2ZFH
Type
protein
Length
643 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cuta
UniProt
O60888
Pockets
11 · best druggability 0.78

Structure

x-ray diffraction · 3 distinct chains · 34% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACutaprotein10933% helix, 41% strandO60888
B, D, E, FCutaprotein10734% helix, 41% strandO60888
CCutaprotein10635% helix, 42% strandO60888

Pockets

11 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14640.780.8680empty
21620.610.8317empty
32810.610.7950empty
41360.590.8417empty
51440.520.8018empty

Interfaces

12 interfaces between chains.

  • D–E · 1227 Ų buried · 18 hydrogen bonds · protein-protein
  • B–C · 1218 Ų buried · 14 hydrogen bonds · protein-protein
  • A–B · 1200 Ų buried · 15 hydrogen bonds · protein-protein
  • E–F · 1173 Ų buried · 14 hydrogen bonds · protein-protein
  • D–F · 1161 Ų buried · 16 hydrogen bonds · protein-protein

Compared structures

  • 2ZFH · Crystal structure of putative CutA1 from Homo sapiens at 2.05A resolution · the same entry in another collection · chain F against F, TM-score 1.00
  • O60888 · AlphaFold monomer V2.0 prediction for protein cuta (O60888) · a predicted model of the same protein · chain C against A, TM-score 0.99

Analyse

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