3F4F
Crystal structure of dUT1p, a dUTPase from Saccharomyces cerevisiae
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004170 | molecular_function | dUTP diphosphatase activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006226 | biological_process | dUMP biosynthetic process |
| A | 0009117 | biological_process | nucleotide metabolic process |
| A | 0009213 | biological_process | pyrimidine deoxyribonucleoside triphosphate catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0035863 | biological_process | dITP catabolic process |
| A | 0035870 | molecular_function | dITP diphosphatase activity |
| A | 0046081 | biological_process | dUTP catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004170 | molecular_function | dUTP diphosphatase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006226 | biological_process | dUMP biosynthetic process |
| B | 0009117 | biological_process | nucleotide metabolic process |
| B | 0009213 | biological_process | pyrimidine deoxyribonucleoside triphosphate catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0035863 | biological_process | dITP catabolic process |
| B | 0035870 | molecular_function | dITP diphosphatase activity |
| B | 0046081 | biological_process | dUTP catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004170 | molecular_function | dUTP diphosphatase activity |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006226 | biological_process | dUMP biosynthetic process |
| C | 0009117 | biological_process | nucleotide metabolic process |
| C | 0009213 | biological_process | pyrimidine deoxyribonucleoside triphosphate catabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0035863 | biological_process | dITP catabolic process |
| C | 0035870 | molecular_function | dITP diphosphatase activity |
| C | 0046081 | biological_process | dUTP catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE UMP B 200 |
| Chain | Residue |
| A | SER69 |
| B | ASP85 |
| B | TYR88 |
| B | VAL92 |
| B | LYS93 |
| B | HOH279 |
| B | HOH308 |
| C | ARG137 |
| C | GLY141 |
| C | PHE142 |
| C | GLY143 |
| A | HOH169 |
| A | HOH174 |
| A | HOH193 |
| A | HOH268 |
| B | ILE65 |
| B | ALA81 |
| B | GLY82 |
| B | VAL83 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE UMP C 200 |
| Chain | Residue |
| A | ARG137 |
| A | GLY141 |
| A | PHE142 |
| A | GLY143 |
| A | HOH158 |
| A | HOH192 |
| A | HOH249 |
| A | HOH264 |
| B | SER69 |
| B | EDO148 |
| C | ILE65 |
| C | ALA81 |
| C | GLY82 |
| C | VAL83 |
| C | ASP85 |
| C | TYR88 |
| C | VAL92 |
| C | LYS93 |
| C | HOH263 |
| C | HOH379 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE UMP A 200 |
| Chain | Residue |
| A | ALA81 |
| A | GLY82 |
| A | VAL83 |
| A | ASP85 |
| A | TYR88 |
| A | VAL92 |
| A | LYS93 |
| A | HOH205 |
| A | HOH211 |
| A | HOH229 |
| A | HOH353 |
| A | HOH376 |
| B | ARG137 |
| B | GLY141 |
| B | PHE142 |
| B | GLY143 |
| B | HOH171 |
| C | SER69 |
| C | PEG148 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO B 148 |
| Chain | Residue |
| A | ARG137 |
| A | HOH249 |
| A | HOH267 |
| B | ASP32 |
| B | GLN114 |
| B | HOH170 |
| B | HOH410 |
| C | UMP200 |
| C | HOH379 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PEG C 148 |
| Chain | Residue |
| A | VAL83 |
| A | ASP85 |
| A | UMP200 |
| A | HOH363 |
| A | HOH376 |
| B | ARG137 |
| C | THR22 |
| C | LYS23 |
| C | GLY24 |
| C | ALA28 |
| C | GLY30 |
| C | ASP32 |
| C | GLN114 |
| C | HOH187 |
| C | HOH460 |
| C | HOH470 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE NA A 148 |
| Chain | Residue |
| A | ARG137 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PEG C 149 |
| Chain | Residue |
| A | ARG102 |
| A | ASP130 |
| A | HOH319 |
| A | HOH432 |
| A | HOH435 |
| A | HOH468 |
| C | GLN12 |
| C | LEU13 |
| C | ARG14 |
| C | HOH416 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 149 |
| Chain | Residue |
| B | LYS119 |
| B | HOH154 |
| C | LYS119 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21548881, ECO:0007744|PDB:3F4F |
| Chain | Residue | Details |
| A | SER69 | |
| B | GLY82 | |
| B | ASP85 | |
| B | TYR88 | |
| B | LYS93 | |
| B | ARG137 | |
| B | PHE142 | |
| B | GLY143 | |
| C | SER69 | |
| C | GLY82 | |
| C | ASP85 | |
| A | GLY82 | |
| C | TYR88 | |
| C | LYS93 | |
| C | ARG137 | |
| C | PHE142 | |
| C | GLY143 | |
| A | ASP85 | |
| A | TYR88 | |
| A | LYS93 | |
| A | ARG137 | |
| A | PHE142 | |
| A | GLY143 | |
| B | SER69 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dup |
| Chain | Residue | Details |
| A | ASP85 | |
| A | ASP87 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dup |
| Chain | Residue | Details |
| B | ASP85 | |
| B | ASP87 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dup |
| Chain | Residue | Details |
| C | ASP85 | |
| C | ASP87 |
