› 2f5j

X-ray diffraction
2.2Å resolution

Crystal structure of MRG domain from human MRG15

Released:
DOI: 10.2210/pdb2f5j/pdb
PDB entry 2f5j coloured by chain, front view.
PDB entry 2f5j coloured by chain, side view.
PDB entry 2f5j coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The MRG domain of human MRG15 uses a shallow hydrophobic pocket to interact with the N-terminal region of PAM14.
Zhang P, Zhao J, Wang B, Du J, Lu Y, Chen J, Ding J
Protein Sci 15 2423-34 (2006)
PMID: 17008723

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193678 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mortality factor 4-like protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 181 amino acids
Theoretical weight: 21.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9UBU8 (Residues: 190-360; Coverage: 47%)
Gene names: FWP006, HSPC008, HSPC061, MORF4L1, MRG15, PP368
Sequence domains: MRG
Structure domains: MRG domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A, PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: R3
Unit cell:
a: 111.151Å b: 111.151Å c: 86.991Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.219 0.205 0.243
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

MRGing chromatin dynamics and cellular senescence.
Garcia et al. (2008)
1 more

3 mentions without citation

The MRG domain of human MRG15 uses a shallow hydrophobic pocket to interact with the N-terminal region of PAM14.
Zhang et al. (2006)
2 more