1M1B
Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0016853 | molecular_function | isomerase activity |
A | 0032923 | biological_process | organic phosphonate biosynthetic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0050188 | molecular_function | phosphoenolpyruvate mutase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0016853 | molecular_function | isomerase activity |
B | 0032923 | biological_process | organic phosphonate biosynthetic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0050188 | molecular_function | phosphoenolpyruvate mutase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 998 |
Chain | Residue |
A | ASP85 |
A | SPV996 |
A | HOH1107 |
A | HOH1108 |
A | HOH1109 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 999 |
Chain | Residue |
B | HOH1112 |
B | ASP85 |
B | SPV997 |
B | HOH1110 |
B | HOH1111 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE SPV A 996 |
Chain | Residue |
A | TRP44 |
A | SER46 |
A | GLY47 |
A | LEU48 |
A | ASP85 |
A | ASN122 |
A | SER123 |
A | LEU124 |
A | ARG159 |
A | HIS190 |
A | MG998 |
A | HOH1107 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE SPV B 997 |
Chain | Residue |
B | TRP44 |
B | SER46 |
B | GLY47 |
B | LEU48 |
B | ASP85 |
B | ASN122 |
B | SER123 |
B | LEU124 |
B | ARG159 |
B | HIS190 |
B | MG999 |
B | HOH1037 |
B | HOH1042 |
B | HOH1112 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000255 |
Chain | Residue | Details |
A | ASP58 | |
B | ASP58 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP58 | |
B | ASP58 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 12 |
Details | M-CSA 271 |
Chain | Residue | Details |
A | SER46 | electrostatic stabiliser, hydrogen bond donor, steric role |
A | SER123 | electrostatic stabiliser, hydrogen bond donor, promote heterolysis |
A | ARG159 | electrostatic stabiliser, hydrogen bond donor, promote heterolysis |
A | HIS190 | electrostatic stabiliser, hydrogen bond donor, promote heterolysis |
A | GLY47 | electrostatic stabiliser, steric role |
A | LEU48 | electrostatic stabiliser, hydrogen bond donor, steric role |
A | ASP58 | metal ligand, nucleofuge, nucleophile, promote heterolysis |
A | ASP85 | electrostatic stabiliser, hydrogen bond donor, metal ligand |
A | ASP87 | electrostatic stabiliser, hydrogen bond donor |
A | GLU114 | electrostatic stabiliser, hydrogen bond donor |
A | LYS120 | electrostatic stabiliser, promote heterolysis |
A | ASN122 | electrostatic stabiliser, hydrogen bond donor, promote heterolysis |
site_id | MCSA2 |
Number of Residues | 12 |
Details | M-CSA 271 |
Chain | Residue | Details |
B | SER46 | electrostatic stabiliser, hydrogen bond donor, steric role |
B | SER123 | electrostatic stabiliser, hydrogen bond donor, promote heterolysis |
B | ARG159 | electrostatic stabiliser, hydrogen bond donor, promote heterolysis |
B | HIS190 | electrostatic stabiliser, hydrogen bond donor, promote heterolysis |
B | GLY47 | electrostatic stabiliser, steric role |
B | LEU48 | electrostatic stabiliser, hydrogen bond donor, steric role |
B | ASP58 | metal ligand, nucleofuge, nucleophile, promote heterolysis |
B | ASP85 | electrostatic stabiliser, hydrogen bond donor, metal ligand |
B | ASP87 | electrostatic stabiliser, hydrogen bond donor |
B | GLU114 | electrostatic stabiliser, hydrogen bond donor |
B | LYS120 | electrostatic stabiliser, promote heterolysis |
B | ASN122 | electrostatic stabiliser, hydrogen bond donor, promote heterolysis |