› 1ihb

X-ray diffraction
1.95Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cyclin-dependent kinase 4 inhibitor C Chains: A, B
Molecule details ›
Chains: A, B
Length: 162 amino acids
Theoretical weight: 17.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P42773 (Residues: 1-162; Coverage: 96%)
Gene names: CDKN2C, CDKN6
Sequence domains: Ankyrin repeats (many copies)
Structure domains: Ankyrin repeat-containing domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 55.51Å b: 151.7Å c: 40.46Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.209 0.289
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

Folding and Stability of Ankyrin Repeats Control Biological Protein Function.
Kumar et al. (2021)
12 more

9 mentions without citation

An Analytical Review of the Structural Features of Pentatricopeptide Repeats: Strategic Amino Acids, Repeat Arrangements and Superhelical Architecture.
Barik S. (2021)
8 more