4ATQ
GABA-transaminase A1R958 in complex with external aldimine PLP-GABA adduct
Summary for 4ATQ
| Entry DOI | 10.2210/pdb4atq/pdb |
| Related | 4ATP |
| Descriptor | 4-AMINOBUTYRATE TRANSAMINASE, PYRIDOXAL-5'-PHOSPHATE, GAMMA-AMINO-BUTANOIC ACID, ... (4 entities in total) |
| Functional Keywords | transferase |
| Biological source | ARTHROBACTER AURESCENS |
| Total number of polymer chains | 12 |
| Total formula weight | 575812.37 |
| Authors | Bruce, H.,Tuan, A.N.,Mangas Sanchez, J.,Hart, S.,Turkenburg, J.P.,Grogan, G. (deposition date: 2012-05-09, release date: 2012-10-10, Last modification date: 2023-12-20) |
| Primary citation | Bruce, H.,Nguyen Tuan, A.,Mangas Sanchez, J.,Leese, C.,Hopwood, J.,Hyde, R.,Hart, S.,Turkenburg, J.P.,Grogan, G. Structures of a Gamma-Aminobutyrate (Gaba) Transaminase from the S-Triazine-Degrading Organism Arthrobacter Aurescens Tc1 in Complex with Plp and with its External Aldimine Plp- Gaba Adduct. Acta Crystallogr.,Sect.F, 68:1175-, 2012 Cited by PubMed Abstract: Two complex structures of the γ-aminobutyrate (GABA) transaminase A1R958 from Arthrobacter aurescens TC1 are presented. The first, determined to a resolution of 2.80 Å, features the internal aldimine formed by reaction between the ℇ-amino group of Lys295 and the cofactor pyridoxal phosphate (PLP); the second, determined to a resolution of 2.75 Å, features the external aldimine adduct formed between PLP and GABA in the first half-reaction. This is the first structure of a microbial GABA transaminase in complex with its natural external aldimine and reveals the molecular determinants of GABA binding in this enzyme. PubMed: 23027742DOI: 10.1107/S1744309112030023 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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