STRUCTURE OF UDP-N-ACETYLGLUCOSAMINE ENOLPYRUVYL TRANSFERASE
The structure was published by Skarzynski, T., Mistry, A., Wonacott, A., Hutchinson, S.E., Kelly, V.A., and Duncan, K., in 1996 in a paper entitled "Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1996.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of UDP-N-ACETYLGLUCOSAMINE ENOLPYRUVYL TRANSFERASE. This molecule has the UniProt identifier P0A749 (MURA_ECOLI). The sample contained 419 residues which is 100% of the natural sequence. Out of 419 residues 418 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: