3RGG
Crystal structure of Treponema denticola PurE bound to AIR
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004638 | molecular_function | phosphoribosylaminoimidazole carboxylase activity |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| B | 0004638 | molecular_function | phosphoribosylaminoimidazole carboxylase activity |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| C | 0004638 | molecular_function | phosphoribosylaminoimidazole carboxylase activity |
| C | 0006164 | biological_process | purine nucleotide biosynthetic process |
| C | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| D | 0004638 | molecular_function | phosphoribosylaminoimidazole carboxylase activity |
| D | 0006164 | biological_process | purine nucleotide biosynthetic process |
| D | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| D | 0016829 | molecular_function | lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE AIR A 1001 |
| Chain | Residue |
| A | GLY10 |
| A | HOH160 |
| A | HOH161 |
| A | HOH162 |
| D | PRO106 |
| D | SER107 |
| A | SER11 |
| A | ASP14 |
| A | SER38 |
| A | HIS40 |
| A | LYS41 |
| A | ALA66 |
| A | GLY67 |
| A | SER69 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE AIR B 1002 |
| Chain | Residue |
| B | GLY10 |
| B | SER11 |
| B | SER13 |
| B | ASP14 |
| B | SER38 |
| B | HIS40 |
| B | LYS41 |
| B | ALA66 |
| B | GLY67 |
| B | ARG68 |
| B | SER69 |
| B | HOH160 |
| B | HOH161 |
| B | HOH162 |
| C | PRO106 |
| C | SER107 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE AIR C 1003 |
| Chain | Residue |
| B | PRO106 |
| B | SER107 |
| C | GLY10 |
| C | SER11 |
| C | SER13 |
| C | ASP14 |
| C | SER38 |
| C | HIS40 |
| C | LYS41 |
| C | ALA66 |
| C | GLY67 |
| C | SER69 |
| C | HOH160 |
| C | HOH161 |
| C | HOH162 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE AIR D 1004 |
| Chain | Residue |
| A | PRO106 |
| A | SER107 |
| D | GLY10 |
| D | SER11 |
| D | SER13 |
| D | ASP14 |
| D | SER38 |
| D | HIS40 |
| D | LYS41 |
| D | ALA66 |
| D | GLY67 |
| D | SER69 |
| D | HOH160 |
| D | HOH161 |
| D | HOH162 |
| D | HOH177 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02045","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21548610","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3RGG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
