4DR9
Crystal structure of a peptide deformylase from synechococcus elongatus in complex with actinonin
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 | BB2203 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE BR A 202 |
Chain | Residue |
A | ARG186 |
D | BR202 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE BB2 A 203 |
Chain | Residue |
A | GLY61 |
A | GLN66 |
A | GLU107 |
A | GLY108 |
A | CYS109 |
A | LEU110 |
A | HIS151 |
A | GLU152 |
A | HIS155 |
A | ZN201 |
A | HOH350 |
A | HOH355 |
B | ARG35 |
A | GLY59 |
A | ILE60 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 201 |
Chain | Residue |
B | GLN66 |
B | CYS109 |
B | HIS151 |
B | HIS155 |
B | BB2203 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BR B 202 |
Chain | Residue |
B | ALA184 |
B | ARG186 |
B | HOH356 |
C | BR203 |
site_id | AC6 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE BB2 B 203 |
Chain | Residue |
A | SER37 |
B | GLY59 |
B | ILE60 |
B | GLY61 |
B | GLN66 |
B | GLY108 |
B | CYS109 |
B | LEU110 |
B | HIS151 |
B | GLU152 |
B | HIS155 |
B | ZN201 |
B | HOH430 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN C 201 |
Chain | Residue |
C | GLN66 |
C | CYS109 |
C | HIS151 |
C | HIS155 |
C | BB2204 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE BR C 202 |
Chain | Residue |
C | SER37 |
C | LYS71 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE BR C 203 |
Chain | Residue |
B | BR202 |
C | ALA184 |
C | ARG186 |
site_id | BC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE BB2 C 204 |
Chain | Residue |
C | GLY59 |
C | ILE60 |
C | GLY61 |
C | GLN66 |
C | GLU107 |
C | GLY108 |
C | CYS109 |
C | LEU110 |
C | TYR116 |
C | ARG147 |
C | HIS151 |
C | GLU152 |
C | HIS155 |
C | ZN201 |
D | ARG35 |
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 | BB2203 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE BR D 202 |
Chain | Residue |
A | ALA184 |
A | BR202 |
D | ALA184 |
D | ARG186 |
D | HOH413 |
site_id | BC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE BB2 D 203 |
Chain | Residue |
D | GLY59 |
D | ILE60 |
D | GLY61 |
D | GLN66 |
D | GLN106 |
D | GLY108 |
D | CYS109 |
D | LEU110 |
D | TYR116 |
D | HIS151 |
D | GLU152 |
D | HIS155 |
D | ZN201 |