1F5S
CRYSTAL STRUCTURE OF PHOSPHOSERINE PHOSPHATASE FROM METHANOCOCCUS JANNASCHII
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 | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 A 220 |
| Chain | Residue |
| A | ASP11 |
| A | HOH222 |
| A | HOH830 |
| A | PHE12 |
| A | ASP13 |
| A | SER99 |
| A | GLY100 |
| A | GLY101 |
| A | LYS144 |
| A | ASN170 |
| A | MG221 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 221 |
| Chain | Residue |
| A | ASP11 |
| A | ASP13 |
| A | ASP167 |
| A | PO4220 |
| A | HOH222 |
| A | HOH223 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 B 720 |
| Chain | Residue |
| B | ASP511 |
| B | PHE512 |
| B | ASP513 |
| B | SER599 |
| B | GLY600 |
| B | LYS644 |
| B | ASN670 |
| B | MG721 |
| B | HOH722 |
| B | HOH943 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 721 |
| Chain | Residue |
| B | ASP511 |
| B | ASP513 |
| B | ASP667 |
| B | PO4720 |
| B | HOH722 |
| B | HOH723 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 230 |
| Chain | Residue |
| A | LYS4 |
| B | ASN548 |
| B | GLU550 |
| B | HOH952 |
| B | HOH962 |
| B | HOH1065 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 B 240 |
| Chain | Residue |
| B | ASN607 |
| B | LYS610 |
| B | GLU611 |
| B | LYS691 |
| B | CYS697 |
| B | GLU699 |
| B | HOH1064 |
| B | HOH1088 |
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 | ASP11 | covalently attached, metal ligand, nucleofuge, nucleophile |
| A | PHE12 | electrostatic stabiliser |
| A | ASP13 | metal ligand, proton acceptor, proton donor |
| A | GLY100 | electrostatic stabiliser |
| A | LYS144 | electrostatic stabiliser |
| A | ASP171 | electrostatic stabiliser, metal ligand |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 727 |
| Chain | Residue | Details |
| B | ASP511 | covalently attached, metal ligand, nucleofuge, nucleophile |
| B | PHE512 | electrostatic stabiliser |
| B | ASP513 | metal ligand, proton acceptor, proton donor |
| B | GLY600 | electrostatic stabiliser |
| B | LYS644 | electrostatic stabiliser |
| B | ASP671 | electrostatic stabiliser, metal ligand |
