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Crystal structure of yeast cyclophilin a, CPR1

Analyse Crystal structure of yeast cyclophilin a, CPR1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1IST
Type: protein
Length: 322 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyclophilin a
EC: 5.2.1.8
UniProt: P14832
Pockets: 2 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cyclophilin a (EC 5.2.1.8)	protein	161	14% helix, 32% strand	P14832

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	199	0.47	0.74	35	empty
2	68	0.33	0.76	19	empty

Interfaces

1 interface between chains.

A–B · 207 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

1IST · Crystal structure of yeast cyclophilin A, CPR1 · the same entry in another collection · chain A against A, TM-score 1.00
P14832 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase (P14832) · a predicted model of the same protein · 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 P14832
Elsewhere: RCSB PDB 1IST · PDBe 1IST · UniProt P14832

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