4GGC: Cell division cycle protein 20 homolog

Structural Analysis of Human Cdc20 Supports Multi-site Degron Recognition by APC/C. Determined by X-ray diffraction at 1.35 Å resolution. Released 7 Nov 2012.

Method: X-ray diffraction
Resolution: 1.35 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,897
Mol. weight: 35.38 kDa
Ligands: MRD
Released: 7 Nov 2012

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

Secondary structure: helices and β-sheets

4GGC 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	392-397	6	7
β-strand	402-408	7	8
β-strand	413-418	6	8
β-strand	425-429	5	8
β-strand	435-439	5	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	318	Homo sapiens	Q12834 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4GGC_1 Cell division cycle protein 20 homolog (chains A)
GSRKTCRYIPSLPDRILDAPEIRNDYYLNLVDWSSGNVLAVALDNSVYLWSASSGDILQL
LQMEQPGEYISSVAWIKEGNYLAVGTSSAEVQLWDVQQQKRLRNMTSHSARVGSLSWNSY
ILSSGSRSGHIHHHDVRVAEHHVATLSGHSQEVCGLRWAPDGRHLASGGNDNLVNVWPSA
PGEGGWVPLQTFTQHQGAVKAVAWCPWQSNVLATGGGTSDRHIRIWNVCSGACLSAVDAH
SQVCSILWSPHYKELISGHGFAQNQLVIWKYPTMAKVAELKGHTSRVLSLTMSPDGATVA
SAAADETLRLWRCFELDP

Ligands and cofactors

ID	Name	Formula	Copies
MRD	(4R)-2-methylpentane-2,4-diol	C6 H14 O2	4

Primary citation

Structural analysis of human Cdc20 supports multisite degron recognition by APC/C. Tian, W., Li, B., Warrington, R. et al. Proc Natl Acad Sci U S A (2012) 109:18419-18424. DOI 10.1073/pnas.1213438109 · PubMed

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

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
4N14 2.1 Å, Crystal structure of Cdc20 and apcin complex
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

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