CRYSTAL STRUCTURE ORNITHINE DECARBOXYLASE FROM MOUSE, TRUNCATED 37 RESIDUES FROM THE C-TERMINUS, TO 1.6 ANGSTROM RESOLUTION
The structure was published by Kern, A.D., Oliveira, M.A., Coffino, P., and Hackert, M.L., in 1999 in a paper entitled "Structure of mammalian ornithine decarboxylase at 1.6 A resolution: stereochemical implications of PLP-dependent amino acid decarboxylases." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.6 Å and deposited in 1999.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of PROTEIN (ORNITHINE DECARBOXYLASE). This molecule has the UniProt identifier P00860 (DCOR_MOUSE). The sample contained 424 residues which is 92% of the natural sequence. Out of 424 residues 386 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 most likely forms homodimers.
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):
This entry contains 1 unique UniProt protein: