4RG9: APC3-APC16 complex

Crystal structure of APC3-APC16 complex (Selenomethionine Derivative). Determined by X-ray diffraction at 3.25 Å resolution. Released 24 Dec 2014.

Method
X-ray diffraction
Resolution
3.25 Å
Organism
Homo sapiens
Chains
3
Atoms
7,542
Mol. weight
134.08 kDa
Released
24 Dec 2014

Explore 4RG9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4RG9 contains 68 α-helices and 0 β-strands across 3 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

ElementResiduesLengthSheet
α-helix8-1710
α-helix21-3414
α-helix38-5013
α-helix54-6310
α-helix69-8113
α-helix85-939
α-helix99-1024
α-helix103-1108
α-helix111-1133
α-helix114-12714
α-helix131-14414
α-helix149-15810
α-helix164-1674
α-helix463-48321
α-helix487-4959
α-helix499-5035
α-helix505-51814
α-helix521-53414
α-helix542-55211
α-helix555-56814
α-helix573-58513
α-helix589-60214
α-helix607-61913
α-helix623-63614
α-helix641-65414
α-helix657-67014
α-helix674-68714
α-helix699-7046
α-helix709-72113
α-helix725-73814
α-helix743-75412
α-helix760-77213
Chain B: 32 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix6-1712
α-helix21-3414
α-helix38-5013
α-helix54-629
α-helix69-8113
α-helix85-928
α-helix100-1023
α-helix103-1108
α-helix111-1133
α-helix114-12714
α-helix131-14414
α-helix150-1578
α-helix164-1674
α-helix463-48321
α-helix487-4948
α-helix499-5024
α-helix505-51713
α-helix521-53414
α-helix543-5519
α-helix555-56612
α-helix573-58513
α-helix589-60214
α-helix607-61913
α-helix623-63614
α-helix641-65313
α-helix657-67014
α-helix674-68714
α-helix700-7045
α-helix709-72113
α-helix725-73814
α-helix743-75614
α-helix759-77214
Chain S: 4 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix75-839
α-helix85-917
α-helix93-953
α-helix99-1024

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Cell division cycle protein 27 homologA, Bprotein560Homo sapiensP30260 (AlphaFold model)
Anaphase-promoting complex subunit 16Sprotein43Homo sapiensQ96DE5 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4RG9_1 Cell division cycle protein 27 homolog (chains A, B)
GSMTVLQEPVQAAIWQALNHYAYRDAVFLAERLYAEVHSEEALFLLATCYYRSGKAYKAY
RLLKGHSCTTPQCKYLLAKCCVDLSKLAEGEQILSGGVFNKQKSHDDIVTEFGDSACFTL
SLLGHVYCKTDRLAKGSECYQKSLSLNPFLWSPFESLCEIGEKPDPDQTFKFTSLQNFSN
CLPQIQAFNLQKAAAEGLMSLLREMGKGYLALCSYNCKEAINILSHLPSHHYNTGWVLCQ
IGRAYFELSEYMQAERIFSEVRRIENYRVEGMEIYSTTLWHLQKDVALSVLSKDLTDMDK
NSPEAWCAAGNCFSLQREHDIAIKFFQRAIQVDPNYAYAYTLLGHEFVLTEELDKALACF
RNAIRVNPRHYNAWYGLGMIYYKQEKFSLAEMHFQKALDINPQSSVLLCHIGVVQHALKK
SEKALDTLNKAIVIDPKNPLCKFHRASVLFANEKYKSALQELEELKQIVPKESLVYFLIG
KVYKKLGQTHLALMNFSWAMDLDPKGANNQIKEAIDKRYLPDDEEPITQEEQIMGTDESQ
ESSMTDADDTQLHAAESDEF
Sequence of entity 2 (S), FASTA
>4RG9_2 Anaphase-promoting complex subunit 16 (chains S)
MQQVARMEKLAGLVEELEADEWRFKPIEQLLGFTPSSENLYFQ

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:

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