4N14: Cdc20 and apcin complex

Crystal structure of Cdc20 and apcin complex. Determined by X-ray diffraction at 2.1 Å resolution. Released 20 Aug 2014.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,538
Mol. weight: 34.88 kDa
Ligands: WR7
Released: 20 Aug 2014

Explore 4N14 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4N14 contains 0 α-helices and 31 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 0 helices, 31 β-strands

Element	Residues	Length	Sheet
β-strand	174-177	4	1
β-strand	188	1	2
β-strand	190-192	3	3
β-strand	197-202	6	3
β-strand	205-210	6	3
β-strand	216-221	6	3
β-strand	229-234	6	2
β-strand	240-245	6	2
β-strand	249-254	6	2
β-strand	259-265	7	2
β-strand	271-277	7	4
β-strand	280-285	6	4
β-strand	289-294	6	4
β-strand	301-306	6	4
β-strand	312-317	6	5
β-strand	323-328	6	5
β-strand	333-337	5	5
β-strand	341	1	6
β-strand	344	1	6
β-strand	349-351	3	5
β-strand	358-363	6	7
β-strand	370-375	6	7
β-strand	381-386	6	7
β-strand	391-397	7	7
β-strand	402-408	7	8
β-strand	413-418	6	8
β-strand	425-429	5	8
β-strand	434-439	6	8
β-strand	446-451	6	1
β-strand	458-462	5	1
β-strand	466-470	5	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cell division cycle protein 20 homolog	A	protein	314	Homo sapiens	Q12834 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4N14_1 Cell division cycle protein 20 homolog (chains A)
GCRYIPSLPDRILDAPEIRNDYYLNLVDWSSGNVLAVALDNSVYLWSASSGDILQLLQME
QPGEYISSVAWIKEGNYLAVGTSSAEVQLWDVQQQKRLRNMTSHSARVGSLSWNSYILSS
GSRSGHIHHHDVRVAEHHVATLSGHSQEVCGLRWAPDGRHLASGGNDNLVNVWPSAPGEG
GWVPLQTFTQHQGAVKAVAWCPWQSNVLATGGGTSDRHIRIWNVCSGACLSAVDAHSQVC
SILWSPHYKELISGHGFAQNQLVIWKYPTMAKVAELKGHTSRVLSLTMSPDGATVASAAA
DETLRLWRCFELDP

Ligands and cofactors

ID	Name	Formula	Copies
WR7	2-(2-methyl-5-nitro-1H-imidazol-1-yl)ethyl [(1R)-2,2,2-trichloro-1-(pyrimidin-2…	C13 H14 Cl3 N7 O4	1

Primary citation

Synergistic blockade of mitotic exit by two chemical inhibitors of the APC/C. Sackton, K.L., Dimova, N., Zeng, X. et al. Nature (2014) 514:646-649. DOI 10.1038/nature13660 · PubMed

Other PDB entries of the same protein (UniProt Q12834 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4GGC 1.35 Å, Structural Analysis of Human Cdc20 Supports Multi-site Degron Recognition by APC/C
9I69 1.46 Å, Crystal structure of human Cdc20 bound to synthetic D-box peptide D20
9I68 1.5 Å, Crystal structure of human Cdc20 bound to synthetic D-box peptide D21
9I6A 1.92 Å, Crystal structure of human Cdc20 bound to synthetic D-box peptide D7
4GGA 2.04 Å, Structural Analysis of Human Cdc20 Supports Multi-site Degron Recognition by APC/C
4GGD 2.44 Å, Structural analysis of human Cdc20 supports multisite degron recognition by APC/C.
6Q6G 3.2 Å, Cryo-EM structure of the APC/C-Cdc20-Cdk2-cyclinA2-Cks2 complex, the D1 box class
6Q6H 3.2 Å, Cryo-EM structure of the APC/C-Cdc20-Cdk2-cyclinA2-Cks2 complex, the D2 box class
6TLJ 3.8 Å, Cryo-EM structure of the Anaphase-promoting complex/Cyclosome, in complex with the…
5G04 3.9 Å, Structure of the human APC-Cdc20-Hsl1 complex
9N9R 3.9 Å, Model of APC/C-CDC20-UBE2C from H2A/H2B-bound complex
9N9S 3.9 Å, Model of APC/C-CDC20-UBE2C from H3/H4-bound complex

Browse structure collections

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