1J97
Phospho-Aspartyl Intermediate Analogue of Phosphoserine phosphatase
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 | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 220 |
| Chain | Residue |
| A | BFD11 |
| A | ASP13 |
| A | ASP167 |
| A | HOH808 |
| A | HOH828 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 720 |
| Chain | Residue |
| B | HOH821 |
| B | BFD511 |
| B | ASP513 |
| B | ASP667 |
| B | HOH809 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 B 230 |
| Chain | Residue |
| B | ASN607 |
| B | LYS610 |
| B | GLU611 |
| B | LYS691 |
| B | CYS697 |
| B | GLU699 |
| B | HOH901 |
| B | HOH1057 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 240 |
| Chain | Residue |
| A | LYS4 |
| B | ASN548 |
| B | GLU550 |
| B | HOH804 |
| B | HOH832 |
| B | HOH928 |
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 | BFD11 | covalently attached, metal ligand, nucleofuge, nucleophile |
| A | LEU16 | electrostatic stabiliser |
| A | VAL17 | metal ligand, proton acceptor, proton donor |
| A | ILE104 | electrostatic stabiliser |
| A | LEU148 | electrostatic stabiliser |
| A | PHE175 | electrostatic stabiliser, metal ligand |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 727 |
| Chain | Residue | Details |
| B | BFD511 | covalently attached, metal ligand, nucleofuge, nucleophile |
| B | LEU516 | electrostatic stabiliser |
| B | VAL517 | metal ligand, proton acceptor, proton donor |
| B | ILE604 | electrostatic stabiliser |
| B | LEU648 | electrostatic stabiliser |
| B | PHE675 | electrostatic stabiliser, metal ligand |
