5LGG: The N-terminal WD40 domain of Apc1

The N-terminal WD40 domain of Apc1 (Anaphase promoting complex subunit 1). Determined by X-ray diffraction at 2.15 Å resolution. Released 5 Oct 2016.

Method: X-ray diffraction
Resolution: 2.15 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,156
Mol. weight: 47.91 kDa
Released: 5 Oct 2016

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

Secondary structure: helices and β-sheets

5LGG contains 10 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: 10 helices, 31 β-strands

Element	Residues	Length	Sheet
β-strand	11-13	3	1
β-strand	15-19	5	2
α-helix	23-27	5
β-strand	72-78	7	3
α-helix	80-82	3
β-strand	89-96	8	3
β-strand	99-106	8	3
β-strand	113-118	6	3
β-strand	125-134	10	4
β-strand	146-154	9	4
β-strand	159-163	5	4
β-strand	168-171	4	4
β-strand	177-183	7	5
β-strand	186-191	6	5
α-helix	192-193	2
α-helix	206-208	3
β-strand	210-213	4	5
α-helix	219-220	2
β-strand	221-222	2	5
β-strand	224-226	3	6
β-strand	237-238	2	6
β-strand	244-250	7	6
β-strand	255-260	6	6
β-strand	265-273	9	6
α-helix	274-275	2
β-strand	407-414	8	6
α-helix	425-427	3
β-strand	429-434	6	7
β-strand	440-446	7	7
α-helix	447-449	3
β-strand	451-459	9	7
β-strand	466-475	10	7
β-strand	478-482	5	1
α-helix	483-485	3
β-strand	487-491	5	1
β-strand	497-501	5	1
β-strand	504-510	7	1
α-helix	517-519	3
β-strand	584-591	8	2
β-strand	594-599	6	2
β-strand	604-608	5	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Anaphase-promoting complex subunit 1,Anaphase-promoting complex subunit 1,Anaphase-promoting…	A	protein	431	Homo sapiens	Q9H1A4 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5LGG_1 Anaphase-promoting complex subunit 1,Anaphase-promoting complex subunit 1,Anaphase-promoting complex subunit 1,Anaphase-promoting complex subunit 1 (chains A)
MSNFYEERTTMIAARDLQEFVPFGRDHCKHHPNGSAGSAQKESWQLRKGVSEIGEDVDYD
EELYVAGNMVIWSKGSKSQALAVYKAFTVDSPVQQALWCDFIISQDKSEKAYSSNEVEKC
ICILQSSCINMHSIEGKDYIASLPFQVANVWPTKYGLLFERSASSHEVPPGSPREPLPTM
FSMLHPLDEITPLVCKSGSLFGSSRVQYVVDHAMKIVFLNTDPSIVMTYDAVQNVHSVWT
LRRVKSEEENVVLKFSEQGGTPQNVATSSSLTAHLRGSIVPELCIDHLWTETITNIREKN
SQASKVFITSDLCGQKFLCFLVESQLQLRCVKFQESNDKTQLIFGSVTNIPAKDAAPVEK
IDTMLVLEGSGNLVLYTGVVRVGKVFIPGLPAPSLTMSGTYIHSIRDPVHNRVTLELSNG
SMVRITIPEIA

Primary citation

WD40 domain of Apc1 is critical for the coactivator-induced allosteric transition that stimulates APC/C catalytic activity. Li, Q., Chang, L., Aibara, S. et al. Proc Natl Acad Sci U S A (2016) 113:10547-10552. DOI 10.1073/pnas.1607147113 · PubMed

Other PDB entries of the same protein (UniProt Q9H1A4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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…
9N9R 3.9 Å, Model of APC/C-CDC20-UBE2C from H2A/H2B-bound complex

Browse structure collections

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