2MAM: Interdigitated double Tudor domain of RBBP1

Solution structure of the interdigitated double Tudor domain of RBBP1. Determined by solution NMR. Released 15 Jan 2014.

Method: Solution NMR
Organism: Homo sapiens
Chains: 1
Atoms: 925
Mol. weight: 13.17 kDa
Released: 15 Jan 2014

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

Secondary structure: helices and β-sheets

2MAM contains 1 α-helix 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: 1 helix, 8 β-strands

Element	Residues	Length	Sheet
β-strand	12-17	6	1
β-strand	20-39	20	1
β-strand	45-49	5	1
β-strand	53-54	2	1
β-strand	62-66	5	1
β-strand	72-90	19	1
β-strand	95-99	5	1
α-helix	100-102	3
β-strand	103	1	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
AT-rich interactive domain-containing protein 4A	A	protein	118	Homo sapiens	P29374 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2MAM_1 AT-rich interactive domain-containing protein 4A (chains A)
ADEPAYLTVGTDVSAKYRGAFCEAKIKTVKRLVKVKVLLKQDNTTQLVQDDQVKGPLRVG
AIVETRTSDGSFQEAIISKLTDASWYTVVFDDGDERTLRRTSLCLKGERHFAESETLD

Primary citation

Retinoblastoma-binding protein 1 has an interdigitated double Tudor domain with DNA binding activity. Gong, W., Wang, J., Perrett, S. et al. J Biol Chem (2014) 289:4882-4895. DOI 10.1074/jbc.M113.501940 · PubMed

Other PDB entries of the same protein (UniProt P29374 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6BPH 1.85 Å, Crystal structure of the chromodomain of RBBP1
7V8N 2.05 Å, Crystal structure of the PWWP-ARID domain of ARID4A
7SMC 2.7 Å, p107 pocket domain complexed with ARID4A peptide
2LCC Solution structure of RBBP1 chromobarrel domain
2YRV Solution structure of the RBB1NT domain of human RB(retinoblastoma)-binding protein 1
6L87 Solution structure of the tandem PWWP-ARID domains of human RBBP1

Browse structure collections

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