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Crystal structure of a mutant PIN1 peptidyl-prolyl cis-trans isomerase

Analyse Crystal structure of a mutant PIN1 peptidyl-prolyl cis-trans isomerase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2ZQU
Type
protein
Length
153 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Peptidyl-prolyl cis-trans isomerase nima-interacting 1
EC
5.2.1.8
UniProt
Q13526
Ligands
SO4
Pockets
1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-prolyl cis-trans isomerase nima-interacting 1 (EC 5.2.1.8)protein15324% helix, 24% strandQ13526

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 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
1800.360.7616SO4

Compared structures

  • 2ZQU · Crystal structure of a mutant PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE · the same entry in another collection · chain A against A, TM-score 1.00

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