TRYPTOPHAN SYNTHASE IN COMPLEX WITH GP, ALPHA-D,L-GLYCEROL-PHOSPHATE, CS, PH6.5 - ALPHA AMINOACRYLATE FORM - (GP)E(A-A)
The structure was published by Ngo, H., Kimmich, N., Harris, R., et al., Barends, T.R., Schlichting, I., and Dunn, M.F., in 2007 in a paper entitled "Allosteric Regulation of Substrate Channeling in Tryptophan Synthase: Modulation of the L-Serine Reaction in Stage I of the Beta-Reaction by Alpha-Site Ligands." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 2006.
The experimental data on which the structure is based was also deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely TRYPTOPHAN SYNTHASE ALPHA CHAIN and TRYPTOPHAN SYNTHASE BETA CHAIN.
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 heterotetramers.
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 2 unique UniProt proteins: