3QLC: Complex structure of ATRX ADD domain

Complex structure of ATRX ADD domain bound to unmodified H3 1-15 peptide. Determined by X-ray diffraction at 2.5 Å resolution. Released 15 Jun 2011.

Method
X-ray diffraction
Resolution
2.5 Å
Organism
Homo sapiens
Chains
4
Atoms
2,236
Mol. weight
33.11 kDa
Ligands
ZN
Released
15 Jun 2011

Explore 3QLC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3QLC contains 12 α-helices and 18 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: 5 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand17011
β-strand17711
β-strand186-18832
β-strand195-19732
α-helix198-2058
β-strand21113
β-strand21713
β-strand228-23144
β-strand238-24034
α-helix241-25717
α-helix262-2643
α-helix271-2733
α-helix274-28512
Chain B: 7 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand17015
β-strand17715
α-helix183-1853
β-strand187-18826
β-strand195-19626
α-helix198-2069
β-strand21117
β-strand21717
β-strand228-23148
β-strand238-24038
α-helix241-2488
α-helix250-2556
α-helix262-2643
α-helix271-2733
α-helix274-28512
Chain C: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand2-544
Chain D: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand3-538

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transcriptional regulator ATRXA, Bprotein129Homo sapiensP46100 (AlphaFold model)
peptide of Histone H3.3C, Dprotein15Homo sapiensP84243 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3QLC_1 Transcriptional regulator ATRX (chains A, B)
GPLGSMGIVSCTACGQQVNHFQKDSIYRHPSLQVLICKNCFKYYMSDDISRDSDGMDEQC
RWCAEGGNLICCDFCHNAFCKKCILRNLGRRELSTIMDENNQWYCYICHPEPLLDLVTAC
NSVYENLEQ
Sequence of entity 2 (C, D), FASTA
>3QLC_2 peptide of Histone H3.3 (chains C, D)
ARTKQTARKSTGGKA

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn6

Primary citation

ATRX ADD domain links an atypical histone methylation recognition mechanism to human mental-retardation syndrome. Iwase, S., Xiang, B., Ghosh, S. et al. Nat Struct Mol Biol (2011) 18:769-776. DOI 10.1038/nsmb.2062 · PubMed

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

Browse structure collections

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