5JG6: Anaphase-promoting complex subunit 11

APC11-Ubv shows role of noncovalent RING-Ubiquitin interactions in processive multiubiquitination and Ubiquitin chain elongation by APC/C. Determined by X-ray diffraction at 2.0 Å resolution. Released 15 Jun 2016.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 4
Atoms: 2,279
Mol. weight: 35 kDa
Ligands: ZN
Released: 15 Jun 2016

Explore 5JG6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5JG6 contains 14 α-helices and 32 β-strands across 4 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.

Chains A and D: 3 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	22	1	1
β-strand	29	1	1
β-strand	46-48	3	2
β-strand	49	1	3
β-strand	54-56	3	2
α-helix	57-66	10
β-strand	72	1	4
α-helix	78	1
β-strand	79	1	4
α-helix	80	1
β-strand	82	1	3

Chain B: 4 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	1-6	6	5
β-strand	12-17	6	5
β-strand	22	1	6
α-helix	23-34	12
α-helix	38-40	3
β-strand	41-45	5	5
β-strand	48-49	2	5
α-helix	50-51	2
β-strand	55	1	6
α-helix	57-59	3
β-strand	66-71	6	5
β-strand	72	1	3

Chain C: 4 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	7
β-strand	12-16	5	7
β-strand	22	1	8
α-helix	23-34	12
α-helix	38-40	3
β-strand	41-45	5	7
β-strand	48-49	2	7
α-helix	50-51	2
β-strand	55	1	8
α-helix	57-59	3
β-strand	66-71	6	7
β-strand	72	1	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Anaphase-promoting complex subunit 11	A, D	protein	70	Homo sapiens	Q9NYG5 (AlphaFold model)
Polyubiquitin-B	B, C	protein	84	Homo sapiens	P0CG47 (AlphaFold model)

Sequence of entity 1 (A, D), FASTA

>5JG6_1 Anaphase-promoting complex subunit 11 (chains A, D)
GSVANDENCGICRMAFNGCCPDCKVPGDDCPLVWGQCSHCFHMHCILKWLHAQQVQQHCP
MCRQEWKFKE

Sequence of entity 2 (B, C), FASTA

>5JG6_2 Polyubiquitin-B (chains B, C)
GSGGSGMQILVKTPRGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQILFFAVKRLEDGR
TLSDYNIQKKSSLLLAMRVPGKMK

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	6

Primary citation

Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C. Brown, N.G., VanderLinden, R., Watson, E.R. et al. Cell (2016) 165:1440-1453. DOI 10.1016/j.cell.2016.05.037 · PubMed

Other PDB entries of the same protein (UniProt Q9NYG5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4R2Y 1.75 Å, Crystal structure of APC11 RING domain
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…
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
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
6TM5 3.9 Å, Cryo-EM structure of the Anaphase-promoting complex/Cyclosome, in complex with the Nek2A…

Browse structure collections

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