6Y20: Protein Scalloped

Name: PDB 6Y20: Crystal structure of Protein Scalloped (222-440) bound to Protein Vestigial (298-337)
Published: 2020-10-21
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transcription

Crystal structure of Protein Scalloped (222-440) bound to Protein Vestigial (298-337). Determined by X-ray diffraction at 1.85 Å resolution. Released 21 Oct 2020.

Method: X-ray diffraction
Resolution: 1.85 Å
Organism: Drosophila melanogaster
Chains: 4
Atoms: 4,273
Mol. weight: 60.78 kDa
Ligands: MYR
Released: 21 Oct 2020

Explore 6Y20 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6Y20 contains 25 α-helices and 26 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: 9 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	226	1	1
β-strand	230-243	14	1
β-strand	246-256	11	1
α-helix	264-266	3
β-strand	267-270	4	2
α-helix	271-273	3
α-helix	275-277	3
α-helix	285-291	7
α-helix	294-296	3
β-strand	297-304	8	2
β-strand	319-328	10	1
β-strand	334-342	9	2
β-strand	345-354	10	2
β-strand	357-359	3	1
β-strand	362-371	10	1
α-helix	372-373	2
α-helix	374-383	10
α-helix	389-397	9
β-strand	399-407	9	2
β-strand	413-423	11	2
α-helix	424-425	2
β-strand	431-438	8	2

Chain B: 10 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	225-226	2	3
β-strand	230-243	14	3
β-strand	246-255	10	3
α-helix	264-266	3
β-strand	267-270	4	2
α-helix	271-273	3
α-helix	275-277	3
α-helix	285-291	7
α-helix	294-296	3
β-strand	297-304	8	2
β-strand	319-328	10	3
α-helix	332-333	2
β-strand	334-342	9	2
β-strand	345-354	10	2
β-strand	357-359	3	3
β-strand	362-371	10	3
α-helix	372-373	2
α-helix	374-384	11
α-helix	389-396	8
β-strand	399-407	9	2
β-strand	413-423	11	2
α-helix	424-425	2
β-strand	431-438	8	2

Chains C and D: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	299-310	12
α-helix	324-326	3
α-helix	331-334	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein scalloped	A	protein	219	Drosophila melanogaster	P30052 (AlphaFold model)
Protein scalloped	B	protein	219	Drosophila melanogaster	P30052 (AlphaFold model)
Protein vestigial	C, D	protein	42	Drosophila melanogaster	Q26366 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6Y20_1 Protein scalloped (chains A)
GRAIATHKFRLLEFTAFMEIQRDEIYHRHLFVQLGGKPSFSDPLLETVDIRQIFDKFPEK
SGGLKDLYEKGPQNAFYLVKCWADLNTDLTTGSETGDFYGVTSQYESNENVVLVCSTIVC
SFGKQVVEXVESEYSRLENNRYVYRIQRSPMCEYMINFIQKLKNLPERYMMNSVLENFTI
LQVMRARETQETLLCIAYVFEVAAQNSGTTHHIYRLIKE

Sequence of entity 2 (B), FASTA

>6Y20_2 Protein scalloped (chains B)
GRAIATHKFRLLEFTAFMEIQRDEIYHRHLFVQLGGKPSFSDPLLETVDIRQIFDKFPEK
SGGLKDLYEKGPQNAFYLVKCWADLNTDLTTGSETGDFYGVTSQYESNENVVLVCSTIVC
SFGKQVVEKVESEYSRLENNRYVYRIQRSPMCEYMINFIQKLKNLPERYMMNSVLENFTI
LQVMRARETQETLLCIAYVFEVAAQNSGTTHHIYRLIKE

Sequence of entity 3 (C, D), FASTA

>6Y20_3 Protein vestigial (chains C, D)
XTASQVDEHFSRALNYNNKDSKESSSPMSNRNFPPSFWNSNX

Ligands and cofactors

ID	Name	Formula	Copies
MYR	Myristic acid	C14 H28 O2	1

Primary citation

A new perspective on the interaction between the Vg/VGLL1-3 proteins and the TEAD transcription factors. Mesrouze, Y., Aguilar, G., Bokhovchuk, F. et al. Sci Rep (2020) 10:17442-17442. DOI 10.1038/s41598-020-74584-x · PubMed

Other PDB entries of the same protein (UniProt P30052 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8A8Q 1.47 Å, Crystal structure of Protein Scalloped in complex with YAP peptide

Browse structure collections

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