1djo Summary

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Crystal structure of Pseudomonas 7A Glutaminase-asparaginase with the inhibitor donv covalently bound in the active site

The structure was published by Ortlund, E., Lacount, M.W., Lewinski, K., and Lebioda, L., in 2000 in a paper entitled "Reactions of Pseudomonas 7A glutaminase-asparaginase with diazo analogues of glutamine and asparagine result in unexpected covalent inhibitions and suggests an unusual catalytic triad Thr-Tyr-Glu." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1999.

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

This PDB entry contains multiple copies of the structure of GLUTAMINASE-ASPARAGINASE.

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 GLUTAMINASE-ASPARAGINASE P10182 (8-337) (ASPQ_PSES7)search Pseudomonas sp. ATCC29598search 98% 330 100%
B GLUTAMINASE-ASPARAGINASE P10182 (8-337) (ASPQ_PSES7)search Pseudomonas sp. ATCC29598search 98% 330 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P10182 (8 - 337) GLUTAMINASE-ASPARAGINASE Pseudomonas sp. 7A

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P10182) Glutaminase/Asparaginasesearch Rossmann foldsearch PF00710: Asparaginasesearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A, B (P10182) asparaginase activitysearch glutamin-(asparagin-)ase activitysearch hydrolase activitysearch cellular amino acid metabolic processsearch asparagine metabolic processsearch periplasmic spacesearch

Chain InterPro annotation
A, B L-asparaginase, type IIsearch Asparaginase/glutaminasesearch Asparaginase/glutaminase, active site 1search L-asparaginase, C-terminal domainsearch L-asparaginase, N-terminalsearch Asparaginase/glutaminase, active site 2search