5C5D
Crystal structure of Treponema denticola PurE2-S38D
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 | 4 |
| Details | binding site for residue EDO A 200 |
| Chain | Residue |
| A | PRO89 |
| A | SER91 |
| A | GLY96 |
| A | HOH356 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 201 |
| Chain | Residue |
| C | ASP137 |
| A | ARG35 |
| B | ASP154 |
| B | LEU157 |
| B | LYS158 |
| C | LYS133 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 200 |
| Chain | Residue |
| B | PRO89 |
| B | PRO90 |
| B | SER91 |
| B | GLY96 |
| B | ILE99 |
| B | HOH369 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 200 |
| Chain | Residue |
| C | PRO89 |
| C | PRO90 |
| C | SER91 |
| C | GLY96 |
| C | HOH386 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO D 200 |
| Chain | Residue |
| C | PHE94 |
| D | PRO89 |
| D | PRO90 |
| D | SER91 |
| D | GLY96 |
| D | HOH362 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02045, ECO:0000269|PubMed:21548610, ECO:0007744|PDB:3RGG |
| Chain | Residue | Details |
| A | SER11 | |
| B | LYS41 | |
| B | GLY67 | |
| B | SER69 | |
| C | SER11 | |
| C | ASP14 | |
| C | ASP38 | |
| C | LYS41 | |
| C | GLY67 | |
| C | SER69 | |
| D | SER11 | |
| A | ASP14 | |
| D | ASP14 | |
| D | ASP38 | |
| D | LYS41 | |
| D | GLY67 | |
| D | SER69 | |
| A | ASP38 | |
| A | LYS41 | |
| A | GLY67 | |
| A | SER69 | |
| B | SER11 | |
| B | ASP14 | |
| B | ASP38 |
