1r6w Summary


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)search. 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):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A o-Succinylbenzoate Synthase P29208 (1-320) (MENC_ECOLI)search Escherichia coli K-12search 100% 322 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P29208 (1 - 320) o-Succinylbenzoate Synthase Escherichia coli

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P29208) D-glucarate dehydratase-likesearch, Enolase N-terminal domain-likesearch Enolase superfamilysearch, Enolase-like, N-terminal domainsearch PF01188: Mandelate racemase / muconate lactonizing enzyme, C-terminal domainsearch

Chain ID Molecular function (GO) Biological process (GO)
A (P29208) hydro-lyase activitysearch catalytic activitysearch magnesium ion bindingsearch lyase activitysearch metal ion bindingsearch menaquinone biosynthetic processsearch metabolic processsearch

Chain InterPro annotation
A Mandelate racemase/muconate lactonizing enzyme/methylaspartate ammonia-lyasesearch O-succinylbenzoic acid (OSB) synthetasesearch Mandelate racemase/muconate lactonizing enzyme, C-terminalsearch Enolase N-terminal domain-likesearch Enolase C-terminal domain-likesearch