Crystal structure of the K133R mutant of o-Succinylbenzoate synthase (OSBS) from Escherichia coli. Complex with SHCHC
The structure was published by Klenchin, V.A., Taylor Ringia, E.A., Gerlt, J.A., and Rayment, I., in 2003 in a paper entitled "Evolution of Enzymatic Activity in the Enolase Superfamily: Structural and Mutagenic Studies of the Mechanism of the Reaction Catalyzed by o-Succinylbenzoate Synthase from Escherichia coli" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.62 Å and deposited in 2003.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of o-Succinylbenzoate Synthase. This molecule has the UniProt identifier P29208 (MENC_ECOLI). The sample contained 322 residues which is 100% of the natural sequence. Out of 322 residues 318 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 homodimers.
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: