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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: 2ZR5
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: 1PG, SO4
Pockets: 1 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase nima-interacting 1 (EC 5.2.1.8)	protein	153	25% helix, 22% strand	Q13526

Ligands and binding sites

1PG · 2-(2-{2-[2-(2-methoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethanol · ligand · chains A
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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	106	0.43	0.77	20	SO4

Compared structures

2ZR5 · 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

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q13526
Elsewhere: RCSB PDB 2ZR5 · PDBe 2ZR5 · UniProt Q13526

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