Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0009396 | biological_process | folic acid-containing compound biosynthetic process |
A | 0016874 | molecular_function | ligase activity |
A | 0030272 | molecular_function | 5-formyltetrahydrofolate cyclo-ligase activity |
A | 0035999 | biological_process | tetrahydrofolate interconversion |
A | 0046872 | molecular_function | metal ion binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0009396 | biological_process | folic acid-containing compound biosynthetic process |
B | 0016874 | molecular_function | ligase activity |
B | 0030272 | molecular_function | 5-formyltetrahydrofolate cyclo-ligase activity |
B | 0035999 | biological_process | tetrahydrofolate interconversion |
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 301 |
Chain | Residue |
A | ARG115 |
A | HOH774 |
A | HOH844 |
A | GLY117 |
A | PHE118 |
A | LYS120 |
A | GLY121 |
A | TYR122 |
A | TYR123 |
A | ADP201 |
A | HOH608 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PO4 B 302 |
Chain | Residue |
B | ARG115 |
B | PHE118 |
B | GLY119 |
B | GLY121 |
B | TYR122 |
B | TYR123 |
B | ADP202 |
B | HOH623 |
B | HOH626 |
B | HOH651 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 401 |
Chain | Residue |
A | ARG115 |
A | ASP124 |
A | ASP154 |
A | ADP201 |
A | HOH612 |
A | HOH773 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 402 |
Chain | Residue |
B | LYS3 |
B | ASP124 |
B | ASP154 |
B | ADP202 |
B | HOH723 |
site_id | AC5 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE ADP A 201 |
Chain | Residue |
A | LYS3 |
A | ARG7 |
A | LEU116 |
A | GLY117 |
A | PHE118 |
A | GLY119 |
A | LYS120 |
A | GLY121 |
A | ASP124 |
A | ARG125 |
A | MET128 |
A | TRP153 |
A | ASP154 |
A | PO4301 |
A | MG401 |
A | HOH608 |
A | HOH612 |
A | HOH628 |
site_id | AC6 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE ADP B 202 |
Chain | Residue |
A | ILE52 |
A | LYS53 |
B | LYS3 |
B | ARG7 |
B | LEU116 |
B | GLY117 |
B | PHE118 |
B | GLY119 |
B | LYS120 |
B | GLY121 |
B | ASP124 |
B | ARG125 |
B | TRP153 |
B | ASP154 |
B | PO4302 |
B | MG402 |
B | HOH606 |
B | HOH626 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS3 | |
A | ARG125 | |
A | TRP153 | |
B | LYS3 | |
B | ARG125 | |
B | TRP153 | |
Chain | Residue | Details |
A | GLU50 | |
A | GLU55 | |
A | ASP124 | |
A | ASP154 | |
B | GLU50 | |
B | GLU55 | |
B | ASP124 | |
B | ASP154 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
A | ARG115 | |
B | ARG115 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | |
Chain | Residue | Details |
A | ARG115 | |
site_id | CSA2 |
Number of Residues | 1 |
Details | |
Chain | Residue | Details |
B | ARG115 | |
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 541 |
Chain | Residue | Details |
A | ARG115 | electrostatic stabiliser, increase electrophilicity |
A | ASP124 | metal ligand |
A | ASP154 | metal ligand |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 541 |
Chain | Residue | Details |
B | ARG115 | electrostatic stabiliser, increase electrophilicity |
B | ASP124 | metal ligand |
B | ASP154 | metal ligand |