1LME
Crystal Structure of Peptide Deformylase from Thermotoga maritima
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006412 | biological_process | translation |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042586 | molecular_function | peptide deformylase activity |
| A | 0043686 | biological_process | co-translational protein modification |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0006412 | biological_process | translation |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0042586 | molecular_function | peptide deformylase activity |
| B | 0043686 | biological_process | co-translational protein modification |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU130 | |
| B | GLU130 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | OCS87 | |
| A | HIS129 | |
| A | HIS133 | |
| B | OCS87 | |
| B | HIS129 | |
| B | HIS133 |
