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Crystal structure of the rrm domain of human SETD1A

Analyse Crystal structure of the rrm domain of human SETD1A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3S8S
Type
protein
Length
107 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Histone-lysine N-methyltransferase SETD1A
UniProt
O15047
Ligands
UNX

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHistone-lysine N-methyltransferase SETD1Aprotein10728% helix, 28% strandO15047

Ligands and binding sites

  • UNX · Unknown atom or ion · ion · 17 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

  • 3S8S · Crystal structure of the RRM domain of human SETD1A · the same entry in another collection · chain A against A, TM-score 1.00
  • O15047 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase SETD1A (O15047) · a predicted model of the same protein · chain A against A, TM-score 0.96

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