4RG7: APC3

Crystal structure of APC3. Determined by X-ray diffraction at 4.25 Å resolution. Released 24 Dec 2014.

Method: X-ray diffraction
Resolution: 4.25 Å
Organism: Homo sapiens
Chains: 2
Atoms: 6,066
Mol. weight: 127.79 kDa
Released: 24 Dec 2014

Explore 4RG7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4RG7 contains 64 α-helices and 0 β-strands across 2 chains. 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: 32 helices, 0 β-strands

Element	Residues	Length
α-helix	6-17	12
α-helix	21-34	14
α-helix	38-50	13
α-helix	54-63	10
α-helix	69-81	13
α-helix	85-92	8
α-helix	99-102	4
α-helix	103-110	8
α-helix	111-113	3
α-helix	114-127	14
α-helix	131-144	14
α-helix	149-158	10
α-helix	164-167	4
α-helix	464-483	20
α-helix	487-496	10
α-helix	500-503	4
α-helix	505-518	14
α-helix	521-534	14
α-helix	542-552	11
α-helix	555-568	14
α-helix	573-585	13
α-helix	589-602	14
α-helix	607-619	13
α-helix	623-636	14
α-helix	641-653	13
α-helix	657-670	14
α-helix	675-687	13
α-helix	698-704	7
α-helix	709-721	13
α-helix	725-738	14
α-helix	743-754	12
α-helix	759-771	13

Chain B: 32 helices, 0 β-strands

Element	Residues	Length
α-helix	7-17	11
α-helix	21-34	14
α-helix	38-50	13
α-helix	54-62	9
α-helix	69-81	13
α-helix	85-92	8
α-helix	101-102	2
α-helix	103-110	8
α-helix	111-113	3
α-helix	114-127	14
α-helix	131-144	14
α-helix	150-157	8
α-helix	164-167	4
α-helix	466-483	18
α-helix	487-494	8
α-helix	499-502	4
α-helix	505-517	13
α-helix	521-534	14
α-helix	543-551	9
α-helix	555-566	12
α-helix	573-585	13
α-helix	589-602	14
α-helix	607-619	13
α-helix	623-636	14
α-helix	641-653	13
α-helix	657-670	14
α-helix	674-686	13
α-helix	700-707	8
α-helix	709-721	13
α-helix	725-738	14
α-helix	743-754	12
α-helix	759-772	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cell division cycle protein 27 homolog	A, B	protein	560	Homo sapiens	P30260 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4RG7_1 Cell division cycle protein 27 homolog (chains A, B)
GSMTVLQEPVQAAIWQALNHYAYRDAVFLAERLYAEVHSEEALFLLATCYYRSGKAYKAY
RLLKGHSCTTPQCKYLLAKCCVDLSKLAEGEQILSGGVFNKQKSHDDIVTEFGDSACFTL
SLLGHVYCKTDRLAKGSECYQKSLSLNPFLWSPFESLCEIGEKPDPDQTFKFTSLQNFSN
CLPQIQAFNLQKAAAEGLMSLLREMGKGYLALCSYNCKEAINILSHLPSHHYNTGWVLCQ
IGRAYFELSEYMQAERIFSEVRRIENYRVEGMEIYSTTLWHLQKDVALSVLSKDLTDMDK
NSPEAWCAAGNCFSLQREHDIAIKFFQRAIQVDPNYAYAYTLLGHEFVLTEELDKALACF
RNAIRVNPRHYNAWYGLGMIYYKQEKFSLAEMHFQKALDINPQSSVLLCHIGVVQHALKK
SEKALDTLNKAIVIDPKNPLCKFHRASVLFANEKYKSALQELEELKQIVPKESLVYFLIG
KVYKKLGQTHLALMNFSWAMDLDPKGANNQIKEAIDKRYLPDDEEPITQEEQIMGTDESQ
ESSMTDADDTQLHAAESDEF

Primary citation

Structure of an APC3-APC16 Complex: Insights into Assembly of the Anaphase-Promoting Complex/Cyclosome. Yamaguchi, M., Yu, S., Qiao, R. et al. J Mol Biol (2015) 427:1748-1764. DOI 10.1016/j.jmb.2014.11.020 · PubMed

Other PDB entries of the same protein (UniProt P30260 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9FGQ 2.5 Å, Structure of human APC3loop 375-381 bound to the NCP
3T1N 2.6 Å, Structure of human MICROCEPHALIN (MCPH1) TANDEM BRCT domains in complex with a CDC27…
9GAW 2.9 Å, High-resolution structure of the Anaphase-promoting complex/cyclosome (APC/C) bound to…
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
8PKP 3.2 Å, Cryo-EM structure of the apo Anaphase-promoting complex/cyclosome (APC/C) at 3.2…
4RG9 3.25 Å, Crystal structure of APC3-APC16 complex (Selenomethionine Derivative)
4RG6 3.3 Å, Crystal structure of APC3-APC16 complex
5G05 3.4 Å, Cryo-EM structure of combined apo phosphorylated APC
8TAU 3.5 Å, APC/C-CDH1-UBE2C-UBE2S-Ubiquitin-CyclinB
4UI9 3.6 Å, Atomic structure of the human Anaphase-Promoting Complex
6TNT 3.78 Å, SUMOylated apoAPC/C with repositioned APC2 WHB domain

Browse structure collections

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