3LUO
Crystal Structure and functional characterization of the thermophilic prolyl isomerase and chaperone SlyD
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
A | 0003824 | molecular_function | catalytic activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0016853 | molecular_function | isomerase activity |
A | 0042026 | biological_process | protein refolding |
A | 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 159 |
Chain | Residue |
A | GLY19 |
A | GLU20 |
A | ALA52 |
A | GLU137 |
A | HOH177 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 160 |
Chain | Residue |
A | HIS145 |
A | HIS147 |
A | HIS149 |
A | HOH163 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 161 |
Chain | Residue |
A | TYR29 |
A | LEU30 |
A | ASN35 |
A | HIS147 |
A | ALA148 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE ZN A 162 |
Chain | Residue |
A | GLU49 |