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Crystal structure of Human ARS2 residues 147-270 + 408-763

Analyse Crystal structure of Human ARS2 residues 147-270 + 408-763 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6F7P
Type
protein
Length
874 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
3.7
Source
Homo sapiens
Molecule
Serrate RNA effector molecule homolog
UniProt
Q9BXP5
Pockets
8 · best druggability 0.70

Structure

x-ray diffraction · resolution 3.7 · 4 distinct chains · 52% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASerrate RNA effector molecule homologprotein12174% helix, 1% strandQ9BXP5
CSerrate RNA effector molecule homologprotein31644% helix, 17% strandQ9BXP5
BSerrate RNA effector molecule homologprotein12274% helix, 1% strandQ9BXP5
DSerrate RNA effector molecule homologprotein31544% helix, 17% strandQ9BXP5

Pockets

8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18270.700.7649empty
27900.690.7644empty
31710.560.8126empty
42210.520.7627empty
51910.500.7727empty

Interfaces

5 interfaces between chains.

  • A–C · 3032 Ų buried · 24 hydrogen bonds · protein-protein
  • B–D · 3019 Ų buried · 22 hydrogen bonds · protein-protein
  • C–D · 320 Ų buried · 4 hydrogen bonds · protein-protein
  • A–D · 260 Ų buried · 0 hydrogen bonds · protein-protein
  • C–B · 114 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 6F7P · Crystal structure of human ARS2 residues 147-270 + 408-763 · the same entry in another collection · chain D against D, TM-score 1.00
  • Q9BXP5 · AlphaFold monomer V2.0 prediction for serrate RNA effector molecule homolog (Q9BXP5) · a predicted model of the same protein · chain D against A, TM-score 0.98

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