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Structure of human cyclophilin a in complex with the novel immunosuppressant sanglifehrin a at 1.6A resolution

Analyse Structure of human cyclophilin a in complex with the novel immunosuppressant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1YND
Type: protein
Length: 328 residues
Chains: 2
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: P62937
Ligands: SFA
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Peptidyl-prolyl cis-trans isomerase a (EC 5.2.1.8)	protein	164	15% helix, 32% strand	P62937

Ligands and binding sites

SFA · Sanglifehrin A · ligand · 2 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1009	0.71	0.75	83	SFA

Interfaces

1 interface between chains.

A–B · 271 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

1YND · Structure of human cyclophilin A in complex with the novel immunosuppressant sanglifehrin… · 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 P62937
Elsewhere: RCSB PDB 1YND · PDBe 1YND · UniProt P62937

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