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Cyclophilin a

Analyse Cyclophilin a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6FK1
Type: protein
Length: 168 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidyl-prolyl cis-trans isomerase a
EC: 5.2.1.8
UniProt: P17742

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase a (EC 5.2.1.8)	protein	168	14% helix, 30% strand	P17742

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 2 copies · chains A

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

Compared structures

6FK1 · Cyclophilin A · the same entry in another collection · chain A against A, TM-score 1.00
P17742 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase a (P17742) · 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 P17742
Elsewhere: RCSB PDB 6FK1 · PDBe 6FK1 · UniProt P17742

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