2LD1: Transcriptional regulator ATRX

Structures and chemical shift assignments for the ADD domain of the ATRX protein. Determined by solution NMR. Released 8 Jun 2011.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
1,131
Mol. weight
16.47 kDa
Ligands
ZN
Released
8 Jun 2011

Explore 2LD1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2LD1 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-strand170-17121
β-strand176-17721
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-helix274-29219

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transcriptional regulator ATRXAprotein142Homo sapiensP46100 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2LD1_1 Transcriptional regulator ATRX (chains A)
GAMADKRGDGLHGIVSCTACGQQVNHFQKDSIYRHPSLQVLICKNCFKYYMSDDISRDSD
GMDEQCRWCAEGGNLICCDFCHNAFCKKCILRNLGRKELSTIMDENNQWYCYICHPEPLL
DLVTACNSVFENLEQLLQQNKK

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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