› 5c0m

X-ray diffraction
1.6Å resolution

Crystal structure of SGF29 tandem tudor domain in complex with a Carba containing peptide

Released:
DOI: 10.2210/pdb5c0m/pdb
PDB entry 5c0m coloured by chain, front view.
PDB entry 5c0m coloured by chain, side view.
PDB entry 5c0m coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Chemical basis for the recognition of trimethyllysine by epigenetic reader proteins.
Kamps JJ, Huang J, Poater J, Xu C, Pieters BJ, Dong A, Min J, Sherman W, Beuming T, Matthias Bickelhaupt F, Li H, Mecinović J
Nat Commun 6 8911 (2015)
PMID: 26578293

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-165483 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
SAGA-associated factor 29 Chains: A, B
Molecule details ›
Chains: A, B
Length: 180 amino acids
Theoretical weight: 20.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q96ES7 (Residues: 115-293; Coverage: 61%)
Gene names: CCDC101, SGF29
Sequence domains: SGF29 tudor-like domain
Structure domains: SH3 type barrels.
Carba-containing peptide Chains: C, D
Molecule details ›
Chains: C, D
Length: 10 amino acids
Theoretical weight: 1.19 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

3 bound ligands:
Ligand SO4 2 x SO4
Ligand UNX 7 x UNX
Ligand GOL 1 x GOL
1 modified residue:
Ligand 4WQ 2 x 4WQ

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P212121
Unit cell:
a: 50.109Å b: 65.193Å c: 105.217Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.204 0.239
Expression systems:
  • Escherichia coli BL21
  • Not provided

Quick links

Citations

9 review citations

Chemical and Biochemical Perspectives of Protein Lysine Methylation.
Luo M. (2018)
8 more

1 mention without citation

Chemical basis for the recognition of trimethyllysine by epigenetic reader proteins.
Kamps et al. (2015)