1rba Summary

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SUBSTITUTION OF ASP193 TO ASN AT THE ACTIVE SITE OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE RESULTS IN CONFORMATIONAL CHANGES

The structure was published by Soderlind, E., Schneider, G., and Gutteridge, S., in 1992 in a paper entitled "Substitution of ASP193 to ASN at the active site of ribulose-1,5-bisphosphate carboxylase results in conformational changes." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.6 Å and deposited in 1991.

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

This PDB entry contains multiple copies of the structure of RUBISCO.

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 RUBISCO P04718 (1-466) (RBL2_RHORU)search Rhodospirillum rubrumsearch 100% 466 95%
B RUBISCO P04718 (1-466) (RBL2_RHORU)search Rhodospirillum rubrumsearch 100% 466 95%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P04718 (1 - 466) RUBISCO Rhodospirillum rubrum

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P04718) RuBisCo, large subunit, C-terminal domainsearch, Ribulose 1,5-bisphosphate carboxylase-oxygenasesearch Alpha-Beta Plaitssearch, Rubiscosearch PF00016: Ribulose bisphosphate carboxylase large chain, catalytic domainsearch, PF02788: Ribulose bisphosphate carboxylase large chain, N-terminal domainsearch

Chain ID Biological process (GO) Molecular function (GO)
A, B (P04718) reductive pentose-phosphate cyclesearch carbon fixationsearch photosynthesissearch oxidation-reduction processsearch ribulose-bisphosphate carboxylase activitysearch lyase activitysearch oxidoreductase activitysearch metal ion bindingsearch magnesium ion bindingsearch monooxygenase activitysearch

Chain InterPro annotation
A, B Ribulose bisphosphate carboxylase, large subunit, C-terminalsearch Ribulose bisphosphate carboxylase, large subunit, ferrodoxin-like N-terminalsearch Ribulose bisphosphate carboxylase, large subunit, N-terminalsearch Ribulose bisphosphate carboxylasesearch