Research workbench

Determination of the NMR solution structure of the cyclophilin a- cyclosporin a complex

Analyse Determination of the NMR solution structure of the cyclophilin a- cyclosporin a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3CYS
Type: protein
Length: 176 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidyl-prolyl cis-trans isomerase a; Cyclosporin a
EC: 5.2.1.8
UniProt: P05092
Pockets: 1 · best druggability 0.34

Structure

solution nmr · 2 distinct chains · 10% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase a (EC 5.2.1.8)	protein	165	11% helix, 27% strand	P05092
B	Cyclosporin a	protein	11	0% helix, 0% 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	72	0.34	0.75	14	empty

Interfaces

1 interface between chains.

A–B · 473 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified, 1 d-amino (nonstandard, methylation, D-amino acid).

Compared structures

3CYS · Determination of the NMR solution structure of the cyclophilin a-cyclosporin a complex · 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 P05092
Elsewhere: RCSB PDB 3CYS · PDBe 3CYS · UniProt P05092

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.