3s8s

X-ray diffraction
1.3Å resolution

Crystal structure of the RRM domain of human SETD1A

Released:
Source organism: Homo sapiens
Entry authors: Chao X, Tempel W, Bian C, Cerovina T, Walker JR, Bountra C, Weigelt J, Arrowsmith CH, Edwards AM, Min J, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine(4) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(4)
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase SETD1A Chain: A
Molecule details ›
Chain: A
Length: 110 amino acids
Theoretical weight: 12.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O15047 (Residues: 89-197; Coverage: 6%)
Gene names: KIAA0339, KMT2F, SET1, SET1A, SETD1A
Sequence domains: RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain)
Structure domains: Alpha-Beta Plaits

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P21
Unit cell:
a: 35.65Å b: 31.51Å c: 39.32Å
α: 90° β: 114.12° γ: 90°
R-values:
R R work R free
0.17 0.168 0.198
Expression system: Escherichia coli