4l1u

X-ray diffraction
2.42Å resolution

Crystal Structure of Human Rtf1 Plus3 Domain in Complex with Spt5 CTR Phosphopeptide

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis for Spt5-mediated recruitment of the Paf1 complex to chromatin.
Proc Natl Acad Sci U S A 110 17290-5 (2013)
PMID: 24101474

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
monomeric
PDBe Complex ID:
PDB-CPX-126214 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
RNA polymerase-associated protein RTF1 homolog Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 138 amino acids
Theoretical weight: 15.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q92541 (Residues: 353-484; Coverage: 19%)
Gene names: KIAA0252, RTF1
Sequence domains: Plus-3 domain
Structure domains: Plus-3 domain
Transcription elongation factor SPT5 Chains: G, H, I, J
Molecule details ›
Chains: G, H, I, J
Length: 13 amino acids
Theoretical weight: 1.47 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: O00267 (Residues: 778-790; Coverage: 1%)
Gene names: SPT5, SPT5H, SUPT5H

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: C2
Unit cell:
a: 112.932Å b: 172.514Å c: 58.476Å
α: 90° β: 107° γ: 90°
R-values:
R R work R free
0.18 0.178 0.226
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided