3ETH
Crystal structure of E. coli Purk in complex with MgATP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004638 | molecular_function | phosphoribosylaminoimidazole carboxylase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0034028 | molecular_function | 5-(carboxyamino)imidazole ribonucleotide synthase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004638 | molecular_function | phosphoribosylaminoimidazole carboxylase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0034028 | molecular_function | 5-(carboxyamino)imidazole ribonucleotide synthase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE ATP A 400 |
| Chain | Residue |
| A | ARG80 |
| A | GLN154 |
| A | ILE156 |
| A | PHE158 |
| A | GLU161 |
| A | HIS184 |
| A | GLU226 |
| A | PHE228 |
| A | ASN237 |
| A | GLU238 |
| A | MG401 |
| A | ILE118 |
| A | MG402 |
| A | HOH664 |
| A | HOH733 |
| A | HOH734 |
| A | HOH735 |
| A | HOH736 |
| A | HOH737 |
| A | HOH738 |
| A | HOH739 |
| A | HOH740 |
| A | LYS120 |
| A | GLY125 |
| A | TYR126 |
| A | ASP127 |
| A | GLY128 |
| A | GLN131 |
| A | GLU153 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | GLU226 |
| A | GLU238 |
| A | ATP400 |
| A | MG402 |
| A | HOH738 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 402 |
| Chain | Residue |
| A | GLU238 |
| A | ATP400 |
| A | MG401 |
| A | HOH734 |
| A | HOH736 |
| site_id | AC4 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE ATP B 400 |
| Chain | Residue |
| B | ARG80 |
| B | ILE118 |
| B | LYS120 |
| B | GLY125 |
| B | TYR126 |
| B | ASP127 |
| B | GLY128 |
| B | GLN131 |
| B | GLU153 |
| B | GLN154 |
| B | GLY155 |
| B | ILE156 |
| B | PHE158 |
| B | GLU161 |
| B | HIS184 |
| B | GLU226 |
| B | PHE228 |
| B | ASN237 |
| B | GLU238 |
| B | MG401 |
| B | MG402 |
| B | HOH524 |
| B | HOH525 |
| B | HOH528 |
| B | HOH649 |
| B | HOH651 |
| B | HOH652 |
| B | HOH653 |
| B | HOH658 |
| B | HOH685 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 401 |
| Chain | Residue |
| B | GLU226 |
| B | GLU238 |
| B | ATP400 |
| B | HOH651 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 402 |
| Chain | Residue |
| B | GLU238 |
| B | ATP400 |
| B | HOH652 |
| B | HOH653 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 366 |
| Details | Domain: {"description":"ATP-grasp","evidences":[{"source":"HAMAP-Rule","id":"MF_01928","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01928","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10569930","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19053251","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
