Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0000166 | molecular_function | nucleotide 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 | 12 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16104022","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
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 |
