| Title | Crystal structure of an aspartate aminotransferase (TM1255) from Thermotoga maritima at 1.90 A resolution. Proteins 55 759-763 2004 | | Site | JCSG | | PDB Id | | Target Id | 283120 | | Molecular Characteristics | | Source | Thermotoga maritima msb8 | | Alias Ids | TPS1273,TM1255 | Molecular Weight | 42418.71 Da. | | Residues | 377 | Isoelectric Point | 6.81 | | Sequence | mvsrriseipisktmeldakakalikkgedvinltagepdfptpepvveeavrflqkgevkytdprgiy elregiakrigerykkdispdqvvvtngakqalfnafmalldpgdevivfspvwvsyipqiilaggtvn vvetfmsknfqpsleevegllvgktkavlinspnnptgvvyrrefleglvrlakkrnfyiisdevydsl vytdeftsildvsegfdrivyingfskshsmtgwrvgylissekvatavskiqshttscintvaqyaal kalevdnsymvqtfkerknfvverlkkmgvkfvepegafylffkvrgddvkfcerlleekkvalvpgsa flkpgfvrlsfatsierltealdriedflnsr | | | BLAST FFAS | | Structure Determination | | Method | XRAY | Chains | 2 | | Resolution (Å) | 1.90 | Rfree | 0.2 | | Matthews' coefficent | 2.31 | Rfactor | 0.159 | | Waters | 587 | Solvent Content | 46.34 |
| Ligand Information | | Ligands | | | Metals | | | |
Protein Summary
The TM1255 from
T. maritima encodes aspartate aminotransferase (EC:2.6.1.1) and its paralog TM1698 belogns to
COG0436 (aspartate/tyrosine/aromatic aminotransferase).
Analysis of the crystallographic packing of TM1255 using the PQS server {Henrick, 1998 #73} indicates that a dimer is the biologically relevant form.
Ligand Summary
References
