4BQ0
Pseudomonas aeruginosa beta-alanine:pyruvate aminotransferase holoenzyme without divalent cations on dimer-dimer interface
Summary for 4BQ0
| Entry DOI | 10.2210/pdb4bq0/pdb |
| Descriptor | BETA-ALANINE--PYRUVATE TRANSAMINASE, CHLORIDE ION, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total) |
| Functional Keywords | transferase, pseudo-translation |
| Biological source | PSEUDOMONAS AERUGINOSA |
| Total number of polymer chains | 4 |
| Total formula weight | 194861.93 |
| Authors | Isupov, M.N.,Lebedev, A.A.,Westlake, A.,Sayer, C.,Littlechild, J.A. (deposition date: 2013-05-29, release date: 2013-06-05, Last modification date: 2023-12-20) |
| Primary citation | Lebedev, A.A.,Isupov, M.N. Space-Group and Origin Ambiguity in Macromolecular Structures with Pseudo-Symmetry and its Treatment with the Program Zanuda. Acta Crystallogr.,Sect.D, 70:2430-, 2014 Cited by PubMed Abstract: The presence of pseudo-symmetry in a macromolecular crystal and its interplay with twinning may lead to an incorrect space-group (SG) assignment. Moreover, if the pseudo-symmetry is very close to an exact crystallographic symmetry, the structure can be solved and partially refined in the wrong SG. Typically, in such incorrectly determined structures all or some of the pseudo-symmetry operations are, in effect, taken for crystallographic symmetry operations and vice versa. A mistake only becomes apparent when the R(free) ceases to decrease below 0.39 and further model rebuilding and refinement cannot improve the refinement statistics. If pseudo-symmetry includes pseudo-translation, the uncertainty in SG assignment may be associated with an incorrect choice of origin, as demonstrated by the series of examples provided here. The program Zanuda presented in this article was developed for the automation of SG validation. Zanuda runs a series of refinements in SGs compatible with the observed unit-cell parameters and chooses the model with the highest symmetry SG from a subset of models that have the best refinement statistics. PubMed: 25195756DOI: 10.1107/S1399004714014795 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.77 Å) |
Structure validation
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