2LXN
Solution NMR structure of glutamine amido transferase subunit of gaunosine monophosphate synthetase from Methanocaldococcus jannaschii
Summary for 2LXN
| Entry DOI | 10.2210/pdb2lxn/pdb |
| NMR Information | BMRB: 17935 |
| Descriptor | GMP synthase [glutamine-hydrolyzing] subunit A (1 entity in total) |
| Functional Keywords | glutamine amidotransferase, ammonia channeling, de-novo purine nucleotide biosynthesis, solution nmr structure, methanocaldococcus jannaschii, ligase |
| Biological source | Methanocaldococcus jannaschii |
| Total number of polymer chains | 1 |
| Total formula weight | 21051.25 |
| Authors | Ali, R.,Kumar, S.,Balaram, H.,Sarma, S.P. (deposition date: 2012-08-30, release date: 2013-06-12, Last modification date: 2024-05-15) |
| Primary citation | Ali, R.,Kumar, S.,Balaram, H.,Sarma, S.P. 1H, 13C, 15N assignment and secondary structure determination of glutamine amido transferase subunit of gaunosine monophosphate synthetase from Methanocaldococcus jannaschii Biomol.Nmr Assign., 6:193-196, 2012 Cited by PubMed Abstract: Sequence specific resonance assignments have been obtained for (1)H, (13)C and (15)N nuclei of the 21 kDa (188 residues long) glutamine amido transferase subunit of guanosine monophosphate synthetase from Methanocaldococcus jannaschii. From an analysis of (1)H and (13)C(α), (13)C(β) secondary chemical shifts, (3) JH(N)H(α) scalar coupling constants and sequential, short and medium range (1)H-(1)H NOEs, it was deduced that the glutamine amido transferase subunit has eleven strands and five helices as the major secondary structural elements in its tertiary structure. PubMed: 22203461DOI: 10.1007/s12104-011-9354-x PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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