4B86: MSL1-MSL2 complex

Crystal structure of the MSL1-MSL2 complex (3.5A). Determined by X-ray diffraction at 3.5 Å resolution. Released 6 Feb 2013.

Method: X-ray diffraction
Resolution: 3.5 Å
Organism: HOMO SAPIENS
Chains: 12
Atoms: 7,042
Mol. weight: 120.74 kDa
Ligands: ZN
Released: 6 Feb 2013

Explore 4B86 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4B86 contains 31 α-helices and 31 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: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	215-259	45

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	215-262	48

Chain C: 5 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	4-18	15
α-helix	27-40	14
β-strand	43	1	1
β-strand	50	1	1
β-strand	55-56	2	2
β-strand	66	1	2
α-helix	68-70	3
α-helix	80-81	2
β-strand	91-92	2	2
α-helix	94-114	21

Chain D: 4 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	4-18	15
α-helix	27-40	14
β-strand	43	1	3
β-strand	50	1	3
α-helix	51	1
β-strand	54-55	2	4
β-strand	66-67	2	4
β-strand	92	1	4
α-helix	94-112	19

Chain E: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	217-263	47

Chain F: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	215-263	49

Chain G: 3 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	4-18	15
α-helix	27-41	15
β-strand	43	1	5
β-strand	50	1	5
β-strand	55	1	6
β-strand	66	1	6
β-strand	92	1	6
α-helix	94-112	19

Chain H: 4 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	4-19	16
α-helix	28-41	14
β-strand	43	1	7
β-strand	50	1	7
β-strand	54-55	2	8
β-strand	66-67	2	8
α-helix	68-70	3
β-strand	92	1	8
α-helix	94-114	21

4 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
Male-specific lethal 1 homolog	A, B, E, F, I, J	protein	59	HOMO SAPIENS	Q68DK7 (AlphaFold model)
Male-specific lethal 2 homolog	C, D, G, H, K, L	protein	116	HOMO SAPIENS	Q9HCI7 (AlphaFold model)

Sequence of entity 1 (A, B, E, F, I, J), FASTA

>4B86_1 MALE-SPECIFIC LETHAL 1 HOMOLOG (chains A, B, E, F, I, J)
GAMGSGASSQAACLKQILLLQLDLIEQQQQQLQAKEKEIEELKSERDTLLARIERMERR

Sequence of entity 2 (C, D, G, H, K, L), FASTA

>4B86_2 MALE-SPECIFIC LETHAL 2 HOMOLOG (chains C, D, G, H, K, L)
MNPVNATALYISASRLVLNYDPGDPKAFTEINRLLPYFRQSLSCCVCGHLLQDPIAPTNS
TCQHYVCKTCKGKKMMMKPSCSWCKDYEQFEENKQLSILVNCYKKLCEYITQTTLA

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	12

Primary citation

Msl1-Mediated Dimerization of the Dosage Compensation Complex is Essential for Male X-Chromosome Regulation in Drosophila. Hallacli, E., Lipp, M., Georgiev, P. et al. Mol Cell (2012) 48:587. DOI 10.1016/J.MOLCEL.2012.09.014 · PubMed

Other PDB entries of the same protein (UniProt Q68DK7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4DNC 2.05 Å, Crystal structure of human MOF in complex with MSL1
4B7Y 3.25 Å, Crystal structure of the MSL1-MSL2 complex

Browse structure collections

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