1gmi Summary



The structure was published by Ochoa, W.F., Garcia-Garcia, J., Fita, I., Corbalan-Garcia, S., Verdaguer, N., and Gomez-Fernandez, J.C., in 2001 in a paper entitled "Structure of the C2 Domain from Novel Protein Kinase Cepsilon. A Membrane Binding Model for Ca(2+ )-Independent C2 Domains" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 2001.

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

The PDB entry contains the structure of PROTEIN KINASE C, EPSILON TYPE. This molecule has the UniProt identifier P09216 (KPCE_RAT)search. The sample contained 136 residues which is < 90% of the natural sequence. Out of 136 residues 133 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 PROTEIN KINASE C, EPSILON TYPE P09216 (1-136) (KPCE_RAT)search Rattus norvegicussearch < 90% 136 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P09216 (1 - 136) PROTEIN KINASE C, EPSILON TYPE Rattus rattus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A PLC-like (P variant)search C2- domain Calcium/lipid binding domainsearch C2 domainsearch
Chain InterPro annotation
A C2 domainsearch