4R2Y: APC11 RING domain

Crystal structure of APC11 RING domain. Determined by X-ray diffraction at 1.75 Å resolution. Released 29 Oct 2014.

Method: X-ray diffraction
Resolution: 1.75 Å
Organism: Homo sapiens
Chains: 4
Atoms: 2,250
Mol. weight: 32.41 kDa
Ligands: ZN
Released: 29 Oct 2014

Explore 4R2Y in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4R2Y contains 12 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.

Chain A: 3 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	22	1	1
β-strand	29	1	1
α-helix	35-37	3
β-strand	46-48	3	2
β-strand	49	1	3
β-strand	54-56	3	2
α-helix	57-67	11
β-strand	72	1	4
β-strand	79	1	4
α-helix	80	1
β-strand	82	1	5

Chain B: 3 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	22	1	6
β-strand	29	1	6
β-strand	46-48	3	7
β-strand	49	1	5
β-strand	54-56	3	7
α-helix	57-67	11
α-helix	68-71	4
β-strand	72	1	8
β-strand	79	1	8
α-helix	80	1
β-strand	82	1	3

Chain C: 4 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	22	1	9
β-strand	29	1	9
β-strand	46-48	3	10
β-strand	49	1	11
β-strand	54-56	3	10
α-helix	57-67	11
α-helix	71	1
β-strand	72	1	12
α-helix	73	1
β-strand	79	1	12
α-helix	80	1
β-strand	82	1	13

Chain D: 2 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	22	1	14
β-strand	29	1	14
β-strand	46-48	3	15
β-strand	49	1	13
β-strand	54-56	3	15
α-helix	57-67	11
α-helix	68-71	4
β-strand	72	1	16
β-strand	79	1	16
β-strand	82	1	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Anaphase-promoting complex subunit 11	A, B, C, D	protein	68	Homo sapiens	Q9NYG5 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>4R2Y_1 Anaphase-promoting complex subunit 11 (chains A, B, C, D)
VANDENCGICRMAFNGCCPDCKVPGDDCPLVWGQCSHCFHMHCILKWLHAQQVQQHCPMC
RQEWKFKE

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	12

Primary citation

Mechanism of Polyubiquitination by Human Anaphase-Promoting Complex: RING Repurposing for Ubiquitin Chain Assembly. Brown, N.G., Watson, E.R., Weissmann, F. et al. Mol Cell (2014) 56:246-260. DOI 10.1016/j.molcel.2014.09.009 · PubMed

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

5JG6 2.0 Å, APC11-Ubv shows role of noncovalent RING-Ubiquitin interactions in processive…
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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