Research workbench

CYCLOPHILIN_5 from C. elegans

Analyse CYCLOPHILIN_5 from C. elegans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1H0P
Type: protein
Length: 182 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidyl-prolyl cis-trans isomerase 5
EC: 5.2.1.8
UniProt: P52013

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase 5 (EC 5.2.1.8)	protein	182	13% helix, 38% strand	P52013

Ligands and binding sites

DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · chains A

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

Compared structures

1H0P · Cyclophilin_5 from C. elegans · the same entry in another collection · chain A against A, TM-score 1.00
P52013 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase 5 (P52013) · 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 P52013
Elsewhere: RCSB PDB 1H0P · PDBe 1H0P · UniProt P52013

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