1uhh Summary


Crystal structure of cp-aequorin

The structure was published by Toma, S., Chong, K.T., Nakagawa, A., Teranishi, K., Inouye, S., and Shimomura, O., in 2005 in a paper entitled "The crystal structures of semi-synthetic aequorins" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 2003.

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

This PDB entry contains multiple copies of the structure of Aequorin 2.

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 has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 Aequorin 2 P02592 (9-196) (AEQ2_AEQVI)search Aequorea victoriasearch 96% 191 100%
B Aequorin 2 P02592 (9-196) (AEQ2_AEQVI)search Aequorea victoriasearch 96% 191 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P02592 (9 - 196) Aequorin 2 Aequorea victoria

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P02592) Calmodulin-likesearch EF-handsearch PF13202: EF handsearch, PF13499: EF-hand domain pairsearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (P02592) metal ion bindingsearch calcium ion bindingsearch bioluminescencesearch

Chain InterPro annotation
A, B EF-hand domainsearch EF-hand domain pairsearch EF-Hand 1, calcium-binding sitesearch