| Title | Crystal structure of a methionine aminopeptidase (TM1478) from Thermotoga maritima at 1.9 A resolution. Proteins 56 396-400 2004 | | Site | JCSG | | PDB Id | | Target Id | 283335 | | Molecular Characteristics | | Source | Thermotoga maritima msb8 | | Alias Ids | TPS1292,TM1478 | Molecular Weight | 27487.50 Da. | | Residues | 250 | Isoelectric Point | 6.62 | | Sequence | miriktpseiekmkkagkavavalrevrkvivpgktawdvetlvleifkklrvkpafkgyggykyatcv svneevvhglplkekvfkegdivsvdvgavyqglygdaavtyivgetdergkelvrvtrevlekaikmi kpgirlgdvshciqetvesvgfnvirdyvghgvgrelhedpqipnygtpgtgvvlrkgmtlaiepmvse gdwrvvvkedgwtavtvdgsrcahfehtilitengaeiltkeg | | | BLAST FFAS | | Structure Determination | | Method | XRAY | Chains | 1 | | Resolution (Å) | 1.90 | Rfree | 0.254 | | Matthews' coefficent | 2.47 | Rfactor | 0.203 | | Waters | 195 | Solvent Content | 50.14 |
| Ligand Information | | Ligands | | | Metals | | | |
Protein Summary
The TM1478 gene of
Thermotoga maritima encodes a methionine aminopeptidase (MAP; EC 3.4.11.18, PubMed:
15211524,
cd01086), that removes the ubiquitous N-terminal methionine from nascent proteins. Methionine aminopeptidases are target proteins for the development of both anticancer and antibacterial
compounds (PubMed:16420038).
Protein encoded by TM1478 has creatinase/aminopeptidase fold (SCOP sunid:55919) with duplication composed of two very similar alpha+beta folds.
Ligand Summary
References