1ec9 Summary

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E. COLI GLUCARATE DEHYDRATASE BOUND TO XYLAROHYDROXAMATE

The structure was published by Gulick, A.M., Hubbard, B.K., Gerlt, J.A., and Rayment, I., in 2000 in a paper entitled "Evolution of enzymatic activities in the enolase superfamily: crystallographic and mutagenesis studies of the reaction catalyzed by D-glucarate dehydratase from Escherichia coli." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2000.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of GLUCARATE DEHYDRATASE.

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 homotetramers.

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 GLUCARATE DEHYDRATASE P0AES2 (1-446) (GUDD_ECOLI)search Escherichia coli K-12search 100% 446 99%
B GLUCARATE DEHYDRATASE P0AES2 (1-446) (GUDD_ECOLI)search Escherichia coli K-12search 100% 446 99%
C GLUCARATE DEHYDRATASE P0AES2 (1-446) (GUDD_ECOLI)search Escherichia coli K-12search 100% 446 99%
D GLUCARATE DEHYDRATASE P0AES2 (1-446) (GUDD_ECOLI)search Escherichia coli K-12search 100% 446 99%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P0AES2 (1 - 446) GLUCARATE DEHYDRATASE Escherichia coli

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C, D (P0AES2) 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, PF13378: Enolase C-terminal domain-likesearch

Chain ID Biological process (GO) Molecular function (GO)
A, B, C, D (P0AES2) glucarate catabolic processsearch metabolic processsearch D-glucarate catabolic processsearch magnesium ion bindingsearch glucarate dehydratase activitysearch catalytic activitysearch metal ion bindingsearch lyase activitysearch

Chain InterPro annotation
A, B, C, D Mandelate racemase/muconate lactonizing enzyme/methylaspartate ammonia-lyasesearch Mandelate racemase/muconate lactonizing enzyme, C-terminalsearch Glucarate dehydratasesearch Enolase N-terminal domain-likesearch Enolase C-terminal domain-likesearch