4brh Summary

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Legionella pneumophila NTPDase1 crystal form II (closed) in complex with MG AND THIAMINE PHOSPHOVANADATE

The structure was published by Zebisch, M., Krauss, M., Schaefer, P., Lauble, P., and Straeter, N., in 2013 in a paper entitled "Crystallographic Snapshots Along the Reaction Pathway of Nucleoside Triphosphate Diphosphohydrolases" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.69 Å and deposited in 2013.

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

This PDB entry contains multiple copies of the structure of ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE I.

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 ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE I Q5ZUA2 (35-393) (Q5ZUA2_LEGPH)search Legionella pneumophila subsp. pneumophila str. Philadelphia 1search 90% 368 98%
B ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE I Q5ZUA2 (35-393) (Q5ZUA2_LEGPH)search Legionella pneumophila subsp. pneumophila str. Philadelphia 1search 90% 368 98%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q5ZUA2 (35 - 393) ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE I Legionella pneumophila

Chain Sequence family (Pfam)
A, B (Q5ZUA2) PF01150: GDA1/CD39 (nucleoside phosphatase) familysearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (Q5ZUA2) hydrolase activitysearch metal ion bindingsearch nucleotide bindingsearch metabolic processsearch

Chain InterPro annotation
A, B Nucleoside phosphatase GDA1/CD39search