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Crystal Structure Analysis of PIN1

Analyse Crystal Structure Analysis of PIN1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6O34
Type
protein
Length
154 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.57
Source
Homo sapiens; SYNTHETIC CONSTRUCT
Molecule
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; peptide
EC
5.2.1.8
UniProt
Q13526
Ligands
SO4
Pockets
1 · best druggability 0.32

Structure

x-ray diffraction · resolution 1.57 · 2 distinct chains · 25% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (EC 5.2.1.8)protein15026% helix, 25% strandQ13526
Bpeptideprotein40% helix, 0% strand—

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains A
  • 2PE · Nonaethylene glycol · additive · chains A
  • GOL · Glycerol · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1540.320.77182PE

Interfaces

1 interface between chains.

  • A–B · 457 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 modified (nonstandard).

Compared structures

  • 6O34 · Crystal structure analysis of PIN1 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q13526 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase… · a predicted model of the same protein · chain A against A, TM-score 0.98

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