CRYSTAL STRUCTURE OF HUMAN ORNITHINE TRANSCARBAMOYLASE COMPLEXED WITH N-PHOSPHONACETYL-L-ORNITHINE
The structure was published by Shi, D., Morizono, H., Ha, Y., Aoyagi, M., Tuchman, M., and Allewell, N.M., in 1998 in a paper entitled "1.85-A resolution crystal structure of human ornithine transcarbamoylase complexed with N-phosphonacetyl-L-ornithine. Catalytic mechanism and correlation with inherited deficiency." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.85 Å and deposited in 1998.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of PROTEIN (ORNITHINE TRANSCARBAMOYLASE). This molecule has the UniProt identifier P00480 (OTC_HUMAN). The sample contained 321 residues which is 91% of the natural sequence. Out of 321 residues 320 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 homotrimers.
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: