1n11 Summary

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D34 REGION OF HUMAN ANKYRIN-R AND LINKER

The structure was published by Michaely, P., Tomchick, D.R., Machius, M., and Anderson, R.G.W., in 2002 in a paper entitled "Crystal structure of a 12 ANK repeat stack from human ankyrinR" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.7 Å and deposited in 2002.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of Ankyrin. This molecule has the UniProt identifier P16157 (ANK1_HUMAN)search. The sample contained 437 residues which is < 90% of the natural sequence. Out of 437 residues 404 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Ankyrin P16157 (402-827) (ANK1_HUMAN)search Homo sapienssearch < 90% 437 92%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P16157 (402 - 827) Ankyrin Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A Ankyrin repeatsearch Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeatsearch Ankyrin repeatsearch
Chain InterPro annotation
A Ankyrin repeatsearch Ankyrin repeat-containing domainsearch