THREE-DIMENSIONAL STRUCTURE OF THE BIFUNCTIONAL ENZYME PHOSPHORIBOSYLANTHRANILATE ISOMERASE: INDOLEGLYCEROLPHOSPHATE SYNTHASE FROM ESCHERICHIA COLI REFINED AT 2.0 ANGSTROMS RESOLUTION
The structure was published by Wilmanns, M., Priestle, J.P., Niermann, T., and Jansonius, J.N., in 1992 in a paper entitled "Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from Escherichia coli refined 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 1991.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of N-(5'PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE. This molecule has the UniProt identifier P00909 (TRPC_ECOLI). The sample contained 452 residues which is 100% of the natural sequence. Out of 452 residues 452 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 is most likely monomeric.
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: