1kcw Summary



The structure was published by Zaitseva, I., Zaitsev, V., Card, G., et al., Bax, B., Ralph, A., and Lindley, P., in 1996 in a paper entitled "The X-ray structure of human serum ceruloplasmin at 3.1 angstrom: Nature of the copper centres." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 3.0 Å and deposited in 1996.

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

The PDB entry contains the structure of CERULOPLASMIN. This molecule has the UniProt identifier P00450 (CERU_HUMAN)search. The sample contained 1046 residues which is 100% of the natural sequence. Out of 1046 residues 1010 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 CERULOPLASMIN P00450 (20-1065) (CERU_HUMAN)search Homo sapienssearch 100% 1046 97%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00450 (20 - 1065) CERULOPLASMIN Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P00450) Multidomain cupredoxinssearch Cupredoxins - blue copper proteinssearch PF00394: Multicopper oxidasesearch, PF07731: Multicopper oxidasesearch, PF07732: Multicopper oxidasesearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A (P00450) cellular iron ion homeostasissearch oxidation-reduction processsearch copper ion transportsearch transmembrane transportsearch ion transportsearch transportsearch oxidoreductase activitysearch copper ion bindingsearch ferroxidase activitysearch chaperone bindingsearch metal ion bindingsearch extracellular regionsearch extracellular spacesearch

Chain InterPro annotation
A Multicopper oxidase, type 1search Multicopper oxidase, copper-binding sitesearch Cupredoxinsearch Multicopper oxidase, type 2search Multicopper oxidase, type 3search Ceruloplasminsearch