2JM1: Transcriptional regulator ATRX

Structures and chemical shift assignments for the ADD domain of the ATRX protein. Determined by solution NMR. Released 26 Jun 2007.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
1,127
Mol. weight
16.41 kDa
Ligands
ZN
Released
26 Jun 2007

Explore 2JM1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2JM1 contains 4 α-helices and 8 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: 4 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand17111
β-strand17611
β-strand187-18822
β-strand195-19622
α-helix198-2069
β-strand21213
β-strand21613
β-strand229-23134
β-strand238-24034
α-helix241-2488
α-helix251-2566
α-helix274-29118

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transcriptional regulator ATRXAprotein141Homo sapiensP46100 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2JM1_1 Transcriptional regulator ATRX (chains A)
GAMKRGEDGLHGIVSCTACGQQVNHFQKDSIYRHPSLQVLICKNCFKYYMSDDISRDSDG
MDEQCRWCAEGGNLICCDFCHNAFCKKCILRNLGRKELSTIMDENNQWYCYICHPEPLLD
LVTACNSVFENLEQLLQQNKK

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn3

Primary citation

Structural consequences of disease-causing mutations in the ATRX-DNMT3-DNMT3L (ADD) domain of the chromatin-associated protein ATRX. Argentaro, A., Yang, J.C., Chapman, L. et al. Proc Natl Acad Sci U S A (2007) 104:11939-11944. DOI 10.1073/pnas.0704057104 · PubMed

Other PDB entries of the same protein (UniProt P46100 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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