2CH0: Human MAN1 C-terminal domain

Solution structure of the human MAN1 C-terminal domain (residues 655- 775). Determined by solution NMR. Released 16 May 2006.

Method: Solution NMR
Organism: HOMO SAPIENS
Chains: 1
Atoms: 1,118
Mol. weight: 15.92 kDa
Released: 16 May 2006

Explore 2CH0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2CH0 contains 5 α-helices and 3 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: 5 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	10-14	5
α-helix	21-35	15
β-strand	45	1	1
α-helix	47-52	6
α-helix	60-63	4
α-helix	64-74	11
β-strand	82-88	7	1
β-strand	91-97	7	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Inner nuclear membrane protein MAN1	A	protein	133	HOMO SAPIENS	Q9Y2U8 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2CH0_1 INNER NUCLEAR MEMBRANE PROTEIN MAN1 (chains A)
GSPEFRWTKEEEETRQMYDMVVKIIDVLRSHNEACQENKDLQPYMPIPHVRDSLIQPHDR
KKMKKVWDRAVDFLAANESRVRTETRRIGGADFLVWRWIQPSASCDKILVIPSKVWQGQA
FHLDRRLERPHRD

Primary citation

The carboxyl-terminal nucleoplasmic region of MAN1 exhibits a DNA binding winged helix domain. Caputo, S., Couprie, J., Duband-Goulet, I. et al. J Biol Chem (2006) 281:18208-18215. DOI 10.1074/jbc.M601980200 · PubMed

Other PDB entries of the same protein (UniProt Q9Y2U8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5ZOJ 2.79 Å, Crystal structure of human SMAD2-MAN1 complex
5ZOK 2.85 Å, Crystal structure of human SMAD1-MAN1 complex.

Browse structure collections

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