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Crystal structure of a peptidyl-prolyl cis-trans isomerase E (ppie) from homo sapiens at 2.50 a resolution

Analyse Crystal structure of a peptidyl-prolyl cis-trans isomerase E (ppie) from homo… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3UCH
Type: protein
Length: 173 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidyl-prolyl cis-trans isomerase E
EC: 5.2.1.8
UniProt: Q9UNP9
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase E (EC 5.2.1.8)	protein	173	13% helix, 31% strand	Q9UNP9

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	63	0.30	0.75	23	empty

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

3UCH · Crystal structure of a peptidyl-prolyl cis-trans isomerase E (PPIE) from Homo sapiens at… · the same entry in another collection · chain A against A, TM-score 1.00
Q9UNP9 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase E (Q9UNP9) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q9UNP9
Elsewhere: RCSB PDB 3UCH · PDBe 3UCH · UniProt Q9UNP9

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