4RN3
Crystal structure of a HAD-superfamily hydrolase, subfamily IA, variant 1 (GSU2069) from Geobacter sulfurreducens PCA at 2.15 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0006281 | biological_process | DNA repair |
| A | 0008967 | molecular_function | phosphoglycolate phosphatase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006281 | biological_process | DNA repair |
| B | 0008967 | molecular_function | phosphoglycolate phosphatase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 301 |
| Chain | Residue |
| A | ASP16 |
| A | ASP18 |
| A | ASP173 |
| A | HOH442 |
| A | HOH452 |
| A | HOH453 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 302 |
| Chain | Residue |
| A | PHE67 |
| A | EDO303 |
| A | GLU50 |
| A | GLN51 |
| A | HIS66 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 303 |
| Chain | Residue |
| A | ARG41 |
| A | PRO42 |
| A | GLN51 |
| A | EDO302 |
| B | ARG143 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 304 |
| Chain | Residue |
| A | SER142 |
| A | ASP209 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 301 |
| Chain | Residue |
| B | ASP16 |
| B | ASP18 |
| B | ASP173 |
| B | SER174 |
| B | ASP177 |
| B | HOH422 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO B 302 |
| Chain | Residue |
| B | LEU128 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 303 |
| Chain | Residue |
| A | SER5 |
| A | GLY108 |
| B | MSE95 |
| B | ARG100 |
| B | PHE129 |
| B | HOH418 |
