6YVH: CWC22-CWC27-EIF4A3 Complex

CWC22-CWC27-EIF4A3 Complex. Determined by X-ray diffraction at 3.19 Å resolution. Released 13 May 2020.

Method: X-ray diffraction
Resolution: 3.19 Å
Organism: Homo sapiens
Chains: 12
Atoms: 14,536
Mol. weight: 237.98 kDa
Released: 13 May 2020

Explore 6YVH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6YVH contains 99 α-helices and 50 β-strands across 12 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: 15 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	132	1	1
α-helix	136-140	5
α-helix	152-172	21
α-helix	178-187	10
α-helix	194-207	14
α-helix	209-211	3
α-helix	212-225	14
α-helix	227-247	21
α-helix	250-265	16
β-strand	269	1	2
α-helix	272-283	12
α-helix	287-307	21
α-helix	309-325	17
α-helix	330-345	16
α-helix	362-364	3
β-strand	368	1	2
α-helix	380-383	4
α-helix	391-402	12

Chain B: 15 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	132	1	3
α-helix	137-140	4
α-helix	152-172	21
α-helix	178-186	9
α-helix	194-207	14
α-helix	209-211	3
α-helix	212-225	14
α-helix	227-247	21
α-helix	250-265	16
β-strand	269	1	4
α-helix	272-283	12
α-helix	287-307	21
α-helix	309-325	17
α-helix	330-345	16
α-helix	362-364	3
β-strand	368	1	4
α-helix	380-383	4
α-helix	391-405	15

Chains C, E and I: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	379-402	24

Chain D: 15 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	132	1	5
α-helix	136-140	5
α-helix	152-172	21
α-helix	178-186	9
α-helix	194-207	14
α-helix	209-211	3
α-helix	212-225	14
α-helix	227-247	21
α-helix	250-265	16
β-strand	269	1	6
α-helix	272-283	12
α-helix	287-307	21
α-helix	309-325	17
α-helix	330-345	16
α-helix	362-364	3
β-strand	368	1	6
α-helix	380-383	4
α-helix	391-402	12

Chain F: 15 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	136-140	5
α-helix	152-172	21
α-helix	178-187	10
α-helix	194-207	14
α-helix	209-211	3
α-helix	212-225	14
α-helix	227-246	20
α-helix	250-265	16
β-strand	269	1	7
α-helix	272-283	12
α-helix	287-307	21
α-helix	309-325	17
α-helix	330-345	16
α-helix	362-364	3
β-strand	368	1	7
α-helix	380-383	4
α-helix	391-405	15

Chain G: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	379-402	24
α-helix	419-421	3

Chains H and J: 8 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	247	1	8
β-strand	252-259	8	9
α-helix	262-274	13
β-strand	279-283	5	9
α-helix	287-299	13
β-strand	304-307	4	9
α-helix	315-324	10
β-strand	330-333	4	9
β-strand	346-351	6	9
α-helix	358-360	3
α-helix	361-365	5
β-strand	367	1	8
β-strand	376-382	7	9
α-helix	386-395	10
β-strand	401-402	2	9
α-helix	403	1
β-strand	404	1	1
α-helix	405-409	5

Chain K: 9 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	247	1	12
β-strand	252-259	8	13
α-helix	261-263	3
α-helix	264-274	11
β-strand	279-283	5	13
α-helix	287-299	13
β-strand	304-307	4	13
α-helix	315-324	10
β-strand	330-333	4	13
β-strand	346-351	6	13
α-helix	358-360	3
α-helix	361-365	5
β-strand	367	1	12
β-strand	376-382	7	13
α-helix	386-395	10
β-strand	401-402	2	13
α-helix	403-404	2
α-helix	405-409	5

1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Pre-mRNA-splicing factor CWC22 homolog	A, B, D, F	protein	291	Homo sapiens	Q9HCG8 (AlphaFold model)
Spliceosome-associated protein CWC27 homolog	C, E, G, I	protein	57	Homo sapiens	Q6UX04 (AlphaFold model)
Eukaryotic initiation factor 4A-III	H, J, K, L	protein	166	Homo sapiens	P38919 (AlphaFold model)

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

>6YVH_1 Pre-mRNA-splicing factor CWC22 homolog (chains A, B, D, F)
RSMKDELDPLLTRTGGAYIPPAKLRMMQEQITDKNSLAYQRMSWEALKKSINGLINKVNI
SNISIIIQELLQENIVRGRGLLSRSVLQAQSASPIFTHVYAALVAIINSKFPQIGELILK
RLILNFRKGYRRNDKQLCLTASKFVAHLINQNVAHEVLCLEMLTLLLERPTDDSVEVAIG
FLKECGLKLTQVSPRGINAIFERLRNILHESEIDKRVQYMIEVMFAVRKDGFKDHPIILE
GLDLVEEDDQFTHMLPLEDDYNPEDVLNVFKMDPNFMENEEKYKAIKKEIL

Sequence of entity 2 (C, E, G, I), FASTA

>6YVH_2 Spliceosome-associated protein CWC27 homolog (chains C, E, G, I)
RSMGTSREDQTLALLNQFKSKLTQAIAETPENDIPETEVEDDEGWMSHVLQFEDKSR

Sequence of entity 3 (H, J, K, L), FASTA

>6YVH_3 Eukaryotic initiation factor 4A-III (chains H, J, K, L)
LTLEGIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKVDWLTEKMREANFTVS
SMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLPNNRELYIHRI
GRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQIDEMPMNVADLI

Primary citation

Structural and functional insights into CWC27/CWC22 heterodimer linking the exon junction complex to spliceosomes. Busetto, V., Barbosa, I., Basquin, J. et al. Nucleic Acids Res (2020) 48:5670-5683. DOI 10.1093/nar/gkaa267 · PubMed

Other PDB entries of the same protein (UniProt Q9HCG8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4C9B 2.0 Å, Crystal structure of eIF4AIII-CWC22 complex
8C6J 2.8 Å, Human spliceosomal PM5 C* complex
7DVQ 2.89 Å, Cryo-EM Structure of the Activated Human Minor Spliceosome (minor Bact Complex)
9XTT 2.92 Å, Human minor spliceosome branching-completed C complex (after step-I)
6ICZ 3.0 Å, Cryo-EM structure of a human post-catalytic spliceosome (P complex) at 3.0 angstrom
8I0R 3.0 Å, The cryo-EM structure of human Bact-I complex
8I0T 3.0 Å, The cryo-EM structure of human Bact-III complex
8I0V 3.0 Å, The cryo-EM structure of human post-Bact complex
9XU3 3.0 Å, Human minor spliceosome exon-ligation-ready C* complex (prior to step-II)
7QTT 3.1 Å, Structural organization of a late activated human spliceosome (Baqr, core region)
6QDV 3.3 Å, Human post-catalytic P complex spliceosome
8I0U 3.3 Å, The cryo-EM structure of human Bact-IV complex

Browse structure collections

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