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 |