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Crystal structure of arabidopsis thaliana cyclophilin 38 (ATCYP38)

Analyse Crystal structure of arabidopsis thaliana cyclophilin 38 (ATCYP38) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3RFY
Type: protein
Length: 356 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidyl-prolyl cis-trans isomerase CYP38, chloroplastic
EC: 5.2.1.8
UniProt: Q9SSA5
Pockets: 6 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase CYP38, chloroplastic (EC 5.2.1.8)	protein	356	30% helix, 20% strand	Q9SSA5

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	69	0.75	0.98	20	empty
2	203	0.51	0.77	20	empty
3	170	0.51	0.78	26	empty
4	151	0.45	0.76	23	empty
5	99	0.39	0.76	21	empty

Compared structures

3RFY · Crystal structure of arabidopsis thaliana cyclophilin 38 (ATCYP38) · the same entry in another collection · chain A against A, TM-score 1.00
Q9SSA5 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase CYP38… · a predicted model of the same protein · chain A against A, TM-score 0.67

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 Q9SSA5
Elsewhere: RCSB PDB 3RFY · PDBe 3RFY · UniProt Q9SSA5

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