MolNFT v1 · #105386 · protein

Structure of the spliceosomal peptidyl-prolyl cis-trans isomerase CWC27 from chaetomium thermophilum

4R3F · Spliceosomal protein CWC27: “Structure of the spliceosomal peptidyl-prolyl cis-trans isomerase CWC27 from chaetomium thermophilum”. X-ray diffraction, 2 pockets (best druggability 0.30). MolNFT v1 #105386 on GenesisL1: 3D structure…

PDB: 4R3F
Type: protein
Length: 196 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Spliceosomal protein CWC27
EC: 5.2.1.8
UniProt: G0RY38
Pockets: 2 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Spliceosomal protein CWC27 (EC 5.2.1.8)	protein	196	16% helix, 24% strand	G0RY38

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 9 copies · chains A
PE5 · 3,6,9,12,15,18,21,24-octaoxahexacosan-1-ol · additive · chains A
ACT · Acetate ion · additive · chains A

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

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	51	0.30	0.77	15	empty
2	51	0.29	0.75	13	EDO

Compared structures

4R3F · Structure of the spliceosomal peptidyl-prolyl cis-trans isomerase Cwc27 from Chaetomium… · the same entry in another collection · 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 G0RY38
Elsewhere: RCSB PDB 4R3F · PDBe 4R3F · UniProt G0RY38

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