EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.6.1.52 | in complex with cofactor pyridoxal 5'-phosphate, to 1.5 A resolution. The enzyme has a fold typical of the aspartate aminotransferase family of pyridoxal phosphate-dependent enzymes. The protein forms a stable symmetrical homodimer which is maintained by extensive interactions, mostly between the large domains of the two subunits. Each active site contains a bound cofactor molecule. The aromatic ring rests above the C-terminal end of the central strand 7 of the seven-stranded beta-sheet in a pocket in which its pyridine N-atom points in towards the interior of the large domain, hydrogen-bonded to the invariant residue Asp176, and its 5'-phosphate and C4 substituent point out into the dimer interface. The phosphate group is adjacent to the N-terminus of helix 3, hydrogen-bonded to the main-chain amide N-atoms of Ala84 and Thr85 and the side chain of Gln199 from one monomer, as well as to Asn251 and Thr252 of the opposing monomer | Mycobacterium tuberculosis |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.6.1.52 | Mycobacterium tuberculosis | P9WQ73 | - |
- |
2.6.1.52 | Mycobacterium tuberculosis H37Rv | P9WQ73 | - |
- |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.6.1.52 | PSAT | - |
Mycobacterium tuberculosis |
2.6.1.52 | serC | - |
Mycobacterium tuberculosis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.6.1.52 | pyridoxal 5'-phosphate | - |
Mycobacterium tuberculosis |