2qyf

X-ray diffraction
2.3Å resolution

Crystal structure of the Mad2/p31(comet)/Mad2-binding peptide ternary complex

Released:
Source organism: Homo sapiens
Primary publication:
p31comet blocks Mad2 activation through structural mimicry.
Cell 131 744-55 (2007)
PMID: 18022368

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-163204 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Mitotic spindle assembly checkpoint protein MAD2A Chains: A, C
Molecule details ›
Chains: A, C
Length: 206 amino acids
Theoretical weight: 23.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13257 (Residues: 1-205; Coverage: 100%)
Gene names: MAD2, MAD2L1
Sequence domains: HORMA domain
Structure domains: HORMA domain
MAD2L1-binding protein Chains: B, D
Molecule details ›
Chains: B, D
Length: 240 amino acids
Theoretical weight: 27.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q15013 (Residues: 36-274; Coverage: 87%)
Gene names: CMT2, KIAA0110, MAD2L1BP
Sequence domains: Mad1 and Cdc20-bound-Mad2 binding
Structure domains: Cell Cycle, Spindle Assembly Checkpoint Protein; Chain A
peptide Chains: E, F
Molecule details ›
Chains: E, F
Length: 12 amino acids
Theoretical weight: 1.45 KDa

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 68.667Å b: 104.519Å c: 138.825Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.187 0.257
Expression system: Escherichia coli BL21(DE3)