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Cyclophilin 3 complexed with dipeptide gly-pro

Analyse Cyclophilin 3 complexed with dipeptide gly-pro in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2IGW
Type: protein
Length: 174 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidyl-prolyl cis-trans isomerase 3
EC: 5.2.1.8
UniProt: P52011
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase 3 (EC 5.2.1.8)	protein	174	13% helix, 30% strand	P52011

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	71	0.34	0.76	17	empty

Compared structures

2IGW · CYCLOPHILIN 3 complexed with DIPEPTIDE GLY-PRO · the same entry in another collection · chain A against A, TM-score 1.00
P52011 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase 3 (P52011) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P52011
Elsewhere: RCSB PDB 2IGW · PDBe 2IGW · UniProt P52011

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