MolNFT v1 · #62752 · protein

Crystal structure of cyclophilin from leishmania donovani ligated with cyclosporin a

3EOV · Peptidyl-prolyl cis-trans isomerase: “Crystal structure of cyclophilin from leishmania donovani ligated with cyclosporin a”. X-ray diffraction, 1 pocket (best druggability 0.31). MolNFT v1 #62752 on GenesisL1: 3D structure, binding…

PDB: 3EOV
Type: protein
Length: 354 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidyl-prolyl cis-trans isomerase; Cyclosporin a
EC: 5.2.1.8
UniProt: Q9U9R3
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 2 distinct chains · 14% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8)	protein	166	15% helix, 34% strand	Q9U9R3
C, D	Cyclosporin a	protein	11	0% helix, 9% strand	—

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	53	0.31	0.77	15	empty

Interfaces

2 interfaces between chains.

A–C · 491 Å² buried · 7 hydrogen bonds · protein-protein
B–D · 488 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified, 2 d-amino (nonstandard, methylation, D-amino acid).

Compared structures

3EOV · Crystal structure of cyclophilin from Leishmania donovani ligated with cyclosporin A · 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 Q9U9R3
Elsewhere: RCSB PDB 3EOV · PDBe 3EOV · UniProt Q9U9R3

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