9FGQ: Human APC3loop 375-381

Structure of human APC3loop 375-381 bound to the NCP. Determined by electron microscopy at 2.5 Å resolution. Released 24 Jul 2024.

Method: Electron microscopy
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 12
Atoms: 11,519
Mol. weight: 336.68 kDa
Released: 24 Jul 2024

Explore 9FGQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9FGQ contains 38 α-helices and 20 β-strands across 8 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 E: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	41-42	2
α-helix	45-54	10
α-helix	64-75	12
β-strand	83-84	2	1
α-helix	86-113	28
β-strand	118-119	2	2
α-helix	121-131	11

Chain B: 4 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	26-28	3
α-helix	31-40	10
β-strand	45-46	2	2
α-helix	50-75	26
β-strand	80-81	2	1
α-helix	83-91	9
β-strand	96-98	3	3

Chains C and G: 6 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	17-21	5
α-helix	27-36	10
β-strand	42-43	2	4
α-helix	47-72	26
β-strand	77-78	2	5
α-helix	80-89	10
α-helix	91-96	6
β-strand	100-102	3	6
α-helix	113-115	3

Chain D: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	35-45	11
β-strand	50-51	2	5
α-helix	53-80	28
β-strand	85-86	2	4
α-helix	88-98	11
α-helix	102-120	19

Chain F: 4 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	26-28	3
α-helix	31-40	10
β-strand	45-46	2	8
α-helix	50-75	26
β-strand	80-81	2	7
α-helix	83-92	10
β-strand	96-98	3	6

Chain H: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	35-45	11
β-strand	50-51	2	10
α-helix	53-80	28
β-strand	85-86	2	9
α-helix	88-98	11
α-helix	101-119	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cell division cycle protein 27 homolog	K, L	protein	317	Homo sapiens	P30260 (AlphaFold model)
Histone H3.1	A, E	protein	136	Homo sapiens	P68431 (AlphaFold model)
Histone H4	B, F	protein	103	Homo sapiens	P62805 (AlphaFold model)
Histone H2A type 2-A	C, G	protein	130	Homo sapiens	Q6FI13 (AlphaFold model)
Histone H2B type 1-B	D, H	protein	273	Homo sapiens	P33778
DNA (132-mer)	I	DNA	211	Homo sapiens
DNA (131-mer)	J	DNA	211	Homo sapiens

Sequence of entity 1 (K, L), FASTA

>9FGQ_1 Cell division cycle protein 27 homolog (chains K, L)
GGSASNCLPNSCTTQVPNHSLSHRQPETVLTETPQDTIELNRLNLESSNSKYSLNTDSSV
SYIDSAVISPDTVPLGTGTSILSKQVQNKPKTGRSLLGGPAALSPLTPSFGILPLETPSP
GDGSYLQNYTNTPPVIDVPSTGAPSKKSVARIGQTGTKSVFSQSGNSREVTPILAQTQSS
GPQTSTTPQVLSPTITSPPNALPRRSSRLFTSDSSTTKENSKKLKMKFPPKIPNRKTKSK
TNKGGITQPNINDSLEITKLDSSIISEGKISTITGSAGSAGSAGSAGSAGSAGSAGSAGS
ARGVPHIVMVDAYKRYK

Sequence of entity 2 (A, E), FASTA

>9FGQ_2 Histone H3.1 (chains A, E)
MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTE
LLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTI
MPKDIQLARRIRGERA

Sequence of entity 3 (B, F), FASTA

>9FGQ_3 Histone H4 (chains B, F)
MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLK
VFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG

Sequence of entity 4 (C, G), FASTA

>9FGQ_4 Histone H2A type 2-A (chains C, G)
MSGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYMAAVLEYLT
AEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKK
TESHHKAKGK

Sequence of entity 5 (D, H), FASTA

>9FGQ_5 Histone H2B type 1-B (chains D, H)
VTTLSGLSGEQGPSGDMTTEEDSATHIKFSKRDEDGRELAGATMELRDSSGKTISTWISD
GHVKDFYLYPGKYTFVETAAPDGYEVATPIEFTVNEDGQVTVDGEATEGDAHTGSAWSHP
QFEKGSAGSAAGSGAGWSHPQFEKGSAMPEPSKSAPAPKKGSKKAITKAQKKDGKKRKRS
RKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSR
EIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK

Sequence of entity 6 (I), FASTA

>9FGQ_6 DNA (132-MER) (chains I)
ATCTTAGCGCGGTGAGTTCAAATACCCGGCAAATCGAGAATCCCGGTGCCGAGGCCGCTC
AATTGGTCGTAGACAGCTCTAGCACCGCTTAAACGCACGTACGCGCTGTCCCCCGCGTTT
TAACCGCCAAGGGGATTACTCCCTAGTCTCCAGGCACGTGTCAGATATATACATCCGATT
TGCCGGGTATTTGAACTCACCGCGCTAAGAT

Sequence of entity 7 (J), FASTA

>9FGQ_7 DNA (131-MER) (chains J)
ATCTTAGCGCGGTGAGTTCAAATACCCGGCAAATCGGATGTATATATCTGACACGTGCCT
GGAGACTAGGGAGTAATCCCCTTGGCGGTTAAAACGCGGGGGACAGCGCGTACGTGCGTT
TAAGCGGTGCTAGAGCTGTCTACGACCAATTGAGCGGCCTCGGCACCGGGATTCTCGATT
TGCCGGGTATTTGAACTCACCGCGCTAAGAT

Primary citation

Spatial control of the APC/C ensures the rapid degradation of cyclin B1. Cirillo, L., Young, R., Veerapathiran, S. et al. EMBO J (2024) 43:4324-4355. DOI 10.1038/s44318-024-00194-2 · PubMed

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

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
6TLJ 3.8 Å, Cryo-EM structure of the Anaphase-promoting complex/Cyclosome, in complex with the…

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