1L7N
TRANSITION STATE ANALOGUE OF PHOSPHOSERINE PHOSPHATASE (ALUMINUM FLUORIDE COMPLEX)
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 | 10 |
| Details | BINDING SITE FOR RESIDUE ALF B 720 |
| Chain | Residue |
| B | ASP511 |
| B | HOH1008 |
| B | PHE512 |
| B | ASP513 |
| B | SER599 |
| B | GLY600 |
| B | LYS644 |
| B | ASN670 |
| B | MG721 |
| B | HOH802 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 721 |
| Chain | Residue |
| B | ASP511 |
| B | ASP513 |
| B | ASP667 |
| B | AF3719 |
| B | ALF720 |
| B | HOH877 |
| B | HOH1008 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ALF A 220 |
| Chain | Residue |
| A | ASP11 |
| A | PHE12 |
| A | ASP13 |
| A | SER99 |
| A | GLY100 |
| A | LYS144 |
| A | ASN170 |
| A | MG221 |
| A | HOH801 |
| A | HOH863 |
| A | HOH895 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 221 |
| Chain | Residue |
| A | ASP11 |
| A | ASP13 |
| A | ASP167 |
| A | AF3219 |
| A | ALF220 |
| A | HOH863 |
| A | HOH895 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 300 |
| Chain | Residue |
| A | ASN48 |
| A | LYS140 |
| A | GLU141 |
| A | HOH813 |
| A | HOH929 |
| A | HOH993 |
| B | LYS504 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AF3 B 719 |
| Chain | Residue |
| B | ASP511 |
| B | PHE512 |
| B | ASP513 |
| B | SER599 |
| B | GLY600 |
| B | LYS644 |
| B | ASN670 |
| B | MG721 |
| B | HOH802 |
| B | HOH877 |
| B | HOH1008 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AF3 A 219 |
| Chain | Residue |
| A | ASP11 |
| A | PHE12 |
| A | ASP13 |
| A | SER99 |
| A | GLY100 |
| A | LYS144 |
| A | ASN170 |
| A | MG221 |
| A | HOH801 |
| A | HOH863 |
| A | HOH895 |
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 | CSA1 |
| Number of Residues | 7 |
| Details | a catalytic site defined by CSA, PubMed 12051918, 10567362 |
| Chain | Residue | Details |
| A | ASP13 | |
| A | ASP13 | |
| A | GLY100 | |
| A | ASP11 | |
| A | LYS144 | |
| A | ASP171 | |
| A | PHE12 |
| site_id | CSA2 |
| Number of Residues | 7 |
| Details | a catalytic site defined by CSA, PubMed 12051918, 10567362 |
| Chain | Residue | Details |
| B | ASP513 | |
| B | ASP513 | |
| B | LYS644 | |
| B | ASP671 | |
| B | PHE512 | |
| B | ASP511 | |
| B | GLY600 |
| 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 |
