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 |