GL1X · GenesisL1 explorer

Research workbench

Crystal structure of protein with unknown function from DUF35 family (13815350) from SULFOLOBUS SOLFATARICUS at 1.80 A resolution

Analyse Crystal structure of protein with unknown function from DUF35 family (13815350)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3IRB
Type
protein
Length
271 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.8
Source
Sulfolobus solfataricus
Molecule
uncharacterized protein from DUF35 family
UniProt
Q97WQ4
Ligands
ZN, SO4
Pockets
2 · best druggability 0.73

Structure

x-ray diffraction · resolution 1.8 · 2 distinct chains · 22% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
Auncharacterized protein from DUF35 familyprotein13723% helix, 40% strandQ97WQ4
Buncharacterized protein from DUF35 familyprotein13420% helix, 41% strandQ97WQ4

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A, B
  • SO4 · Sulfate ion · ion · 6 copies · chains A, B
  • ACY · Acetic acid · additive · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13080.730.8639SO4
21260.710.9127SO4

Interfaces

1 interface between chains.

  • A–B · 1124 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

  • 3IRB · Crystal structure of protein with unknown function from DUF35 family (13815350) from… · 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.