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The structure of reduced cyclophilin A from s. mansoni

Analyse The structure of reduced cyclophilin A from s. mansoni in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2CMT
Type: protein
Length: 164 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.5
Source: SCHISTOSOMA MANSONI
Molecule: Peptidyl-prolyl cis-trans isomerase E
EC: 5.2.1.8
UniProt: Q26548
Pockets: 1 · best druggability 0.35

Structure

x-ray diffraction · resolution 1.5 · 1 distinct chain · 15% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase E (EC 5.2.1.8)	protein	164	15% helix, 34% strand	Q26548

Ligands and binding sites

ACT · Acetate ion · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	90	0.35	0.75	22	empty

Compared structures

2CMT · The structure of reduced cyclophilin a from S. mansoni · the same entry in another collection · chain A against A, TM-score 1.00
Q26548 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase E (Q26548) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q26548
Elsewhere: RCSB PDB 2CMT · PDBe 2CMT · UniProt Q26548

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