1L7O
CRYSTAL STRUCTURE OF PHOSPHOSERINE PHOSPHATASE IN APO FORM
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006564 | biological_process | L-serine biosynthetic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0036424 | molecular_function | L-phosphoserine phosphatase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006564 | biological_process | L-serine biosynthetic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0036424 | molecular_function | L-phosphoserine phosphatase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 301 |
| Chain | Residue |
| A | CYS197 |
| A | GLU199 |
| B | CYS697 |
| B | GLU699 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 302 |
| Chain | Residue |
| A | GLU79 |
| A | GLU146 |
| A | GLU149 |
| A | ACY312 |
| A | HOH2045 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 303 |
| Chain | Residue |
| B | ACY311 |
| B | GLU579 |
| B | GLU646 |
| B | GLU649 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACY B 311 |
| Chain | Residue |
| B | ZN303 |
| B | GLU579 |
| B | GLY580 |
| B | GLU583 |
| B | GLU646 |
| B | HOH2060 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACY A 312 |
| Chain | Residue |
| A | GLU79 |
| A | GLY80 |
| A | GLU83 |
| A | GLU146 |
| A | ZN302 |
| A | HOH2045 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"11342136","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11438683","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12051918","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"11342136","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11438683","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12051918","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11342136","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11438683","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12051918","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12051918","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 727 |
| Chain | Residue | Details |
| A | THR15 | covalently attached, metal ligand, nucleofuge, nucleophile |
| A | LEU16 | electrostatic stabiliser |
| A | VAL17 | metal ligand, proton acceptor, proton donor |
| A | LYS108 | electrostatic stabiliser |
| A | ALA152 | electrostatic stabiliser |
| A | GLY179 | electrostatic stabiliser, metal ligand |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 727 |
| Chain | Residue | Details |
| B | THR515 | covalently attached, metal ligand, nucleofuge, nucleophile |
| B | LEU516 | electrostatic stabiliser |
| B | VAL517 | metal ligand, proton acceptor, proton donor |
| B | LYS608 | electrostatic stabiliser |
| B | ALA652 | electrostatic stabiliser |
| B | GLY679 | electrostatic stabiliser, metal ligand |
