CRYSTAL STRUCTURE ANALYSIS, REFINEMENT AND ENZYMATIC REACTION MECHANISM OF N-CARBAMOYLSARCOSINE AMIDOHYDROLASE FROM ARTHROBACTER SP. AT 2.0 ANGSTROMS RESOLUTION
The structure was published by Romao, M.J., Turk, D., Gomis-Ruth, F.X., et al., Schumacher, G., Mollering, H., and Russmann, L., in 1992 in a paper entitled "Crystal structure analysis, refinement and enzymatic reaction mechanism of N-carbamoylsarcosine amidohydrolase from Arthrobacter sp. at 2.0 A resolution." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1992.
The experimental data on which the structure is based was not deposited.
This PDB entry contains multiple copies of the structure of N-CARBAMOYLSARCOSINE AMIDOHYDROLASE.
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 homotetramers.
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: