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Structure of the spliceosomal peptidyl-prolyl cis-trans isomerase CWC27 from homo sapiens

Analyse Structure of the spliceosomal peptidyl-prolyl cis-trans isomerase CWC27 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4R3E
Type: protein
Length: 173 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidyl-prolyl cis-trans isomerase CWC27 homolog
EC: 5.2.1.8
UniProt: Q6UX04
Pockets: 1 · best druggability 0.27

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase CWC27 homolog (EC 5.2.1.8)	protein	173	16% helix, 29% strand	Q6UX04

Ligands and binding sites

GOL · Glycerol · additive · 3 copies · chains A

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

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	54	0.27	0.75	18	GOL

Compared structures

4R3E · Structure of the spliceosomal peptidyl-prolyl cis-trans isomerase Cwc27 from Homo sapiens · the same entry in another collection · chain A against A, TM-score 1.00
Q6UX04 · AlphaFold monomer V2.0 prediction for spliceosome-associated protein CWC27 homolog… · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q6UX04
Elsewhere: RCSB PDB 4R3E · PDBe 4R3E · UniProt Q6UX04

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