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Crystal structure of CDC20 and apcin complex

Analyse Crystal structure of CDC20 and apcin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4N14
Type: protein
Length: 313 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division cycle protein 20 homolog
UniProt: Q12834
Ligands: WR7
Pockets: 3 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell division cycle protein 20 homolog	protein	313	0% helix, 52% strand	Q12834

Ligands and binding sites

WR7 · 2-(2-methyl-5-nitro-1H-imidazol-1-yl)ethyl [(1R)-2,2,2-trichloro-1-(pyrimidin-2-ylamino)ethyl]carbamate · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	571	0.73	0.81	45	empty
2	55	0.41	0.81	11	WR7
3	51	0.27	0.74	13	empty

Compared structures

4N14 · Crystal structure of Cdc20 and apcin complex · the same entry in another collection · chain A against A, TM-score 1.00
Q12834 · AlphaFold monomer V2.0 prediction for cell division cycle protein 20 homolog (Q12834) · 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 Q12834
Elsewhere: RCSB PDB 4N14 · PDBe 4N14 · UniProt Q12834

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