Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006188 | biological_process | IMP biosynthetic process |
| A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006188 | biological_process | IMP biosynthetic process |
| B | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 401 |
| Chain | Residue |
| A | SER10 |
| A | SER71 |
| A | HIS75 |
| A | ARG238 |
| A | SER240 |
| A | HOH642 |
| A | HOH668 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 A 402 |
| Chain | Residue |
| A | ARG287 |
| A | ALA290 |
| A | HOH612 |
| A | HOH644 |
| A | HOH664 |
| A | HOH665 |
| A | HOH667 |
| A | HIS11 |
| A | ARG202 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 600 |
| Chain | Residue |
| A | GLU98 |
| A | GLU104 |
| A | ILE284 |
| A | HOH601 |
| A | HOH673 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 401 |
| Chain | Residue |
| B | SER10 |
| B | SER71 |
| B | HIS75 |
| B | ARG238 |
| B | SER240 |
| B | HOH603 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 402 |
| Chain | Residue |
| B | HIS11 |
| B | ARG202 |
| B | ARG287 |
| B | ALA290 |
| B | HOH611 |
| B | HOH618 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA B 600 |
| Chain | Residue |
| B | GLU98 |
| B | GLU104 |
| B | ILE284 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ATP A 400 |
| Chain | Residue |
| A | PRO116 |
| A | LYS132 |
| A | ALA136 |
| A | GLY138 |
| A | TYR142 |
| A | GLN173 |
| A | GLU174 |
| A | TYR175 |
| A | PHE282 |
| A | GLU283 |
| A | HOH663 |
| A | HOH687 |
| A | HOH691 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ATP B 400 |
| Chain | Residue |
| B | PRO116 |
| B | LYS132 |
| B | TYR142 |
| B | GLN173 |
| B | GLU174 |
| B | ARG212 |
| B | TYR227 |
| B | PHE282 |
| B | HOH642 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 500 |
| Chain | Residue |
| A | ILE130 |
| A | TYR142 |
| A | ASP217 |
| A | TYR227 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD A 501 |
| Chain | Residue |
| A | TYR175 |
| A | LEU177 |
| A | PHE221 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 247 |
| Details | Domain: {"description":"ATP-grasp","evidences":[{"source":"HAMAP-Rule","id":"MF_01163","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01163","evidenceCode":"ECO:0000255"}]} |
