1v8s Summary


Crystal structure analusis of the ADP-ribose pyrophosphatase complexed with AMP and Mg

The structure was published by Yoshiba, S., Ooga, T., Nakagawa, N., et al., Yokoyama, S., Kuramitsu, S., and Masui, R., in 2004 in a paper entitled "Structural insights into the Thermus thermophilus ADP-ribose pyrophosphatase mechanism via crystal structures with the bound substrate and metal" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 2004.

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

The PDB entry contains the structure of ADP-ribose pyrophosphatase. This molecule has the UniProt identifier Q84CU3 (Q84CU3_THETH)search. The sample contained 170 residues which is 100% of the natural sequence. Out of 170 residues 152 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 ADP-ribose pyrophosphatase Q84CU3 (1-170) (Q84CU3_THETH)search Thermus thermophilussearch 100% 170 89%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q84CU3 (1 - 170) ADP-ribose pyrophosphatase Thermus thermophilus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (Q84CU3) MutT-likesearch Nucleoside Triphosphate Pyrophosphohydrolasesearch PF00293: NUDIX domainsearch

Chain ID Molecular function (GO) Biological process (GO)
A (Q84CU3) hydrolase activitysearch nucleotide bindingsearch metabolic processsearch

Chain InterPro annotation
A NUDIX hydrolase domainsearch NUDIX hydrolase domain-likesearch NUDIX hydrolase, conserved sitesearch NUDIX hydrolasesearch