1mns Summary

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ON THE ROLE OF LYSINE 166 IN THE MECHANISM OF MANDELATE RACEMASE FROM PSEUDOMONAS PUTIDA: MECHANISTIC AND CRYSTALLOGRAPHIC EVIDENCE FOR STEREOSPECIFIC ALKYLATION BY (R)-ALPHA-PHENYLGLYCIDATE

The structure was published by Landro, J.A., Gerlt, J.A., Kozarich, J.W., et al., Neidhart, D.J., Fujita, S., and Petsko, G.A., in 1994 in a paper entitled "The role of lysine 166 in the mechanism of mandelate racemase from Pseudomonas putida: mechanistic and crystallographic evidence for stereospecific alkylation by (R)-alpha-phenylglycidate." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1993.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of MANDELATE RACEMASE. This molecule has the UniProt identifier P11444 (MANR_PSEPU)search. The sample contained 357 residues which is 99% of the natural sequence. Out of 357 residues 357 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 homooctamers.

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 MANDELATE RACEMASE P11444 (3-359) (MANR_PSEPU)search Pseudomonas putidasearch 99% 357 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P11444 (3 - 359) MANDELATE RACEMASE Pseudomonas putida

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P11444) D-glucarate dehydratase-likesearch, Enolase N-terminal domain-likesearch Enolase-like, N-terminal domainsearch, Enolase superfamilysearch PF01188: Mandelate racemase / muconate lactonizing enzyme, C-terminal domainsearch, PF02746: Mandelate racemase / muconate lactonizing enzyme, N-terminal domainsearch

Chain ID Molecular function (GO) Biological process (GO)
A (P11444) catalytic activitysearch mandelate racemase activitysearch isomerase activitysearch metal ion bindingsearch cellular amino acid catabolic processsearch metabolic processsearch mandelate metabolic processsearch mandelate catabolic processsearch

Chain InterPro annotation
A Mandelate racemase/muconate lactonizing enzyme/methylaspartate ammonia-lyasesearch Mandelate racemase/muconate lactonizing enzyme, N-terminal domainsearch Mandelate racemase/muconate lactonizing enzyme, C-terminalsearch Mandelate racemase/muconate lactonizing enzyme, conserved sitesearch Enolase N-terminal domain-likesearch Enolase C-terminal domain-likesearch