GL1X · GenesisL1 explorer

Research workbench

Crystal structure analysis of the mutant CUTA1 (E61V) from E. COLI

Analyse Crystal structure analysis of the mutant CUTA1 (E61V) from E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3AA9
Type
protein
Length
311 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Divalent-cation tolerance protein cuta
UniProt
P69488
Pockets
4 · best druggability 0.78

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
ADivalent-cation tolerance protein cutaprotein10436% helix, 42% strandP69488
BDivalent-cation tolerance protein cutaprotein10335% helix, 43% strandP69488
CDivalent-cation tolerance protein cutaprotein10433% helix, 42% strandP69488

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1910.780.9818empty
21720.590.8219empty
3830.580.8715empty
41130.570.8416empty

Interfaces

3 interfaces between chains.

  • A–B · 1105 Ų buried · 15 hydrogen bonds · protein-protein
  • A–C · 1096 Ų buried · 10 hydrogen bonds · protein-protein
  • B–C · 1061 Ų buried · 16 hydrogen bonds · protein-protein

Compared structures

  • 3AA9 · Crystal Structure Analysis of the Mutant CutA1 (E61V) from E. coli · the same entry in another collection · chain B against B, TM-score 1.00
  • P69488 · AlphaFold monomer V2.0 prediction for divalent-cation tolerance protein cuta (P69488) · a predicted model of the same protein · chain A 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.