7odc Summary

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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)search. 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):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A PROTEIN (ORNITHINE DECARBOXYLASE) P00860 (1-424) (DCOR_MOUSE)search Mus musculussearch 92% 424 91%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00860 (1 - 424) PROTEIN (ORNITHINE DECARBOXYLASE) Mus musculus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P00860) Eukaryotic ODC-likesearch, Alanine racemase-like, N-terminal domainsearch Lyase, Ornithine Decarboxylase; Chain A, domain 1search, Alanine racemasesearch PF00278: Pyridoxal-dependent decarboxylase, C-terminal sheet domainsearch, PF02784: Pyridoxal-dependent decarboxylase, pyridoxal binding domainsearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P00860) catalytic activitysearch lyase activitysearch ornithine decarboxylase activitysearch carboxy-lyase activitysearch protein homodimerization activitysearch polyamine metabolic processsearch polyamine biosynthetic processsearch putrescine biosynthetic processsearch response to virussearch kidney developmentsearch regulation of protein catabolic processsearch putrescine biosynthetic process from ornithinesearch positive regulation of cell proliferationsearch cytoplasmsearch cytosolsearch perinuclear region of cytoplasmsearch

Chain InterPro annotation
A Ornithine/DAP/Arg decarboxylasesearch Ornithine decarboxylasesearch Alanine racemase/group IV decarboxylase, C-terminalsearch Orn/DAP/Arg decarboxylase 2, C-terminalsearch Orn/DAP/Arg decarboxylase 2, N-terminalsearch Orn/DAP/Arg decarboxylase 2, pyridoxal-phosphate binding sitesearch Orn/DAP/Arg decarboxylase 2, conserved sitesearch PLP-binding barrelsearch