4DR8
Crystal structure of a peptide deformylase from Synechococcus elongatus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006412 | biological_process | translation |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0018206 | biological_process | peptidyl-methionine modification |
| A | 0042586 | molecular_function | peptide deformylase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0006412 | biological_process | translation |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0018206 | biological_process | peptidyl-methionine modification |
| B | 0042586 | molecular_function | peptide deformylase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0006412 | biological_process | translation |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0018206 | biological_process | peptidyl-methionine modification |
| C | 0042586 | molecular_function | peptide deformylase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0006412 | biological_process | translation |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0018206 | biological_process | peptidyl-methionine modification |
| D | 0042586 | molecular_function | peptide deformylase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 201 |
| Chain | Residue |
| A | GLN66 |
| A | CYS109 |
| A | HIS151 |
| A | HIS155 |
| A | FMT203 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 202 |
| Chain | Residue |
| D | GLN183 |
| D | ALA184 |
| D | ARG186 |
| A | GLN183 |
| A | ALA184 |
| A | ARG186 |
| A | HOH382 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FMT A 203 |
| Chain | Residue |
| A | GLY61 |
| A | GLN66 |
| A | CYS109 |
| A | LEU110 |
| A | HIS151 |
| A | GLU152 |
| A | HIS155 |
| A | ZN201 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 201 |
| Chain | Residue |
| B | CYS109 |
| B | HIS151 |
| B | HIS155 |
| B | FMT204 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 202 |
| Chain | Residue |
| B | ALA10 |
| B | GLN52 |
| B | HOH490 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 203 |
| Chain | Residue |
| A | GLN106 |
| A | TYR116 |
| A | HOH446 |
| B | LYS34 |
| B | ARG35 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FMT B 204 |
| Chain | Residue |
| B | GLY61 |
| B | GLN66 |
| B | CYS109 |
| B | LEU110 |
| B | HIS151 |
| B | GLU152 |
| B | HIS155 |
| B | ZN201 |
| B | HOH459 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 201 |
| Chain | Residue |
| C | CYS109 |
| C | HIS151 |
| C | HIS155 |
| C | FMT203 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO C 202 |
| Chain | Residue |
| B | GLN183 |
| B | ALA184 |
| B | ARG186 |
| B | HOH320 |
| C | GLN183 |
| C | ALA184 |
| C | ARG186 |
| C | HOH334 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FMT C 203 |
| Chain | Residue |
| C | GLY61 |
| C | GLN66 |
| C | CYS109 |
| C | LEU110 |
| C | HIS151 |
| C | GLU152 |
| C | HIS155 |
| C | ZN201 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 201 |
| Chain | Residue |
| D | GLN66 |
| D | CYS109 |
| D | HIS151 |
| D | HIS155 |
| D | FMT202 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FMT D 202 |
| Chain | Residue |
| D | GLY61 |
| D | GLN66 |
| D | CYS109 |
| D | LEU110 |
| D | HIS151 |
| D | GLU152 |
| D | HIS155 |
| D | ZN201 |
| D | HOH493 |
