1e3p Summary

pdbe.org/1e3p
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TUNGSTATE DERIVATIVE OF STREPTOMYCES ANTIBIOTICUS PNPASE/ GPSI ENZYME

The structure was published by Symmons, M.F., Jones, G.H., and Luisi, B.F., in 2000 in a paper entitled "A Duplicated Fold is the Structural Basis for Polynucleotide Phosphorylase Catalytic Activity, Processivity, and Regulation" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 2000.

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

The PDB entry contains the structure of GUANOSINE PENTAPHOSPHATE SYNTHETASE.

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 homotrimers.

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 GUANOSINE PENTAPHOSPHATE SYNTHETASE Q53597 (1-665) (PNP_STRAT)search Streptomyces antibioticussearch 90% 757 85%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q53597 (1 - 665) GUANOSINE PENTAPHOSPHATE SYNTHETASE Streptomyces antibioticus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (Q53597) Polynucleotide phosphorylase/guanosine pentaphosphate synthase (PNPase/GPSI), domain 3search, Cold shock DNA-binding domain-likesearch, Ribonuclease PH domain 1-likesearch, Prokaryotic type KH domain (KH-domain type II)search, Ribonuclease PH domain 2-likesearch GHMP Kinase, N-terminal domainsearch, Arc Repressor Mutant, subunit Asearch PF00013: KH domainsearch, PF00575: S1 RNA binding domainsearch, PF01138: 3' exoribonuclease family, domain 1search, PF03725: 3' exoribonuclease family, domain 2search, PF03726: Polyribonucleotide nucleotidyltransferase, RNA binding domainsearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A (Q53597) transferase activitysearch nucleotidyltransferase activitysearch metal ion bindingsearch 3'-5'-exoribonuclease activitysearch RNA bindingsearch polyribonucleotide nucleotidyltransferase activitysearch magnesium ion bindingsearch cytoplasmsearch mRNA catabolic processsearch RNA processingsearch RNA phosphodiester bond hydrolysis, exonucleolyticsearch

Chain InterPro annotation
A Exoribonuclease, phosphorolytic domain 1search Ribosomal protein S1, RNA-binding domainsearch K Homology domainsearch K Homology domain, type 1search Polyribonucleotide nucleotidyltransferasesearch Nucleic acid-binding, OB-foldsearch Guanosine pentaphosphate synthetase I/polyribonucleotide nucleotidyltransferasesearch Exoribonuclease, phosphorolytic domain 2search Polyribonucleotide nucleotidyltransferase, RNA-binding domainsearch Ribosomal protein S5 domain 2-type foldsearch RNA-binding domain, S1search PNPase/RNase PH domainsearch