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Crystal Structure of the PRYSPRY-domain

Analyse Crystal Structure of the PRYSPRY-domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2FBE
Type
protein
Length
775 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.52
Source
Homo sapiens
Molecule
PREDICTED: similar to ret finger protein-like 1
Pockets
11 · best druggability 0.55

Structure

x-ray diffraction · resolution 2.52 · 4 distinct chains · 3% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APREDICTED: similar to ret finger protein-like 1protein1882% helix, 40% strand—
BPREDICTED: similar to ret finger protein-like 1protein1984% helix, 36% strand—
CPREDICTED: similar to ret finger protein-like 1protein1994% helix, 36% strand—
DPREDICTED: similar to ret finger protein-like 1protein1903% helix, 39% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12030.550.7933empty
22100.550.7836empty
32120.530.7837empty
42410.530.7630empty
51560.520.8029empty

Interfaces

4 interfaces between chains.

  • C–D · 671 Ų buried · 10 hydrogen bonds · protein-protein
  • A–B · 645 Ų buried · 13 hydrogen bonds · protein-protein
  • B–D · 362 Ų buried · 5 hydrogen bonds · protein-protein
  • A–C · 344 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

  • 2FBE · Crystal structure of the pryspry-domain · the same entry in another collection · chain A against A, TM-score 1.00

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