1RMD: RAG1 dimerization domain

RAG1 dimerization domain. Determined by X-ray diffraction at 2.1 Å resolution. Released 23 Jul 1997.

Method
X-ray diffraction
Resolution
2.1 Å
Organism
Mus musculus
Chains
1
Atoms
967
Mol. weight
13.41 kDa
Ligands
ZN
Released
23 Jul 1997

Explore 1RMD in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1RMD contains 9 α-helices and 10 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: 9 helices, 10 β-strands

ElementResiduesLengthSheet
α-helix2-43
α-helix9-113
β-strand1211
α-helix18-236
β-strand2512
β-strand3212
β-strand36-3833
β-strand44-4633
α-helix47-5610
β-strand6014
β-strand6714
α-helix70-723
β-strand7413
α-helix75-773
α-helix78-869
β-strand88-9031
β-strand99-10131
α-helix102-1109
α-helix113-1142

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
RAG1Aprotein116Mus musculusP15919 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1RMD_1 RAG1 (chains A)
NCSKIHLSTKLLAVDFPAHFVKSISCQICEHILADPVETSCKHLFCRICILRCLKVMGSY
CPSCRYPCFPTDLESPVKSFLNILNSLMVKCPAQDCNEEVSLEKYNHHVSSHKESK

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn4

Primary citation

Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster. Bellon, S.F., Rodgers, K.K., Schatz, D.G. et al. Nat Struct Biol (1997) 4:586-591. DOI 10.1038/nsb0797-586 · PubMed

Other PDB entries of the same protein (UniProt P15919 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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