3EHW
Human dUTPase in complex with alpha,beta-imido-dUTP and Mg2+: visualization of the full-length C-termini in all monomers and suggestion for an additional metal ion binding site
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004170 | molecular_function | dUTP diphosphatase activity |
A | 0006226 | biological_process | dUMP biosynthetic process |
A | 0046081 | biological_process | dUTP catabolic process |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004170 | molecular_function | dUTP diphosphatase activity |
B | 0006226 | biological_process | dUMP biosynthetic process |
B | 0046081 | biological_process | dUTP catabolic process |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0004170 | molecular_function | dUTP diphosphatase activity |
C | 0006226 | biological_process | dUMP biosynthetic process |
C | 0046081 | biological_process | dUTP catabolic process |
X | 0000287 | molecular_function | magnesium ion binding |
X | 0004170 | molecular_function | dUTP diphosphatase activity |
X | 0006226 | biological_process | dUMP biosynthetic process |
X | 0046081 | biological_process | dUTP catabolic process |
Y | 0000287 | molecular_function | magnesium ion binding |
Y | 0004170 | molecular_function | dUTP diphosphatase activity |
Y | 0006226 | biological_process | dUMP biosynthetic process |
Y | 0046081 | biological_process | dUTP catabolic process |
Z | 0000287 | molecular_function | magnesium ion binding |
Z | 0004170 | molecular_function | dUTP diphosphatase activity |
Z | 0006226 | biological_process | dUMP biosynthetic process |
Z | 0046081 | biological_process | dUTP catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE DUP C 777 |
Chain | Residue |
A | ARG85 |
B | VAL100 |
B | ILE101 |
B | ASP102 |
B | TYR105 |
B | GLY110 |
B | HOH778 |
C | ARG153 |
C | GLY157 |
C | PHE158 |
C | GLY159 |
A | SER86 |
C | SER160 |
C | THR161 |
C | HOH780 |
C | HOH857 |
X | HOH790 |
X | HOH856 |
A | GLY87 |
A | GLN131 |
A | MG165 |
A | HOH850 |
A | HOH854 |
B | ALA98 |
B | GLY99 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 165 |
Chain | Residue |
A | HOH850 |
A | HOH854 |
C | DUP777 |
C | HOH857 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG C 778 |
Chain | Residue |
B | DUP777 |
B | HOH849 |
C | HOH855 |
X | HOH874 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG B 165 |
Chain | Residue |
A | DUP777 |
B | HOH796 |
B | HOH856 |
X | HOH888 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG Z 165 |
Chain | Residue |
Y | DUP777 |
Y | HOH854 |
Z | HOH779 |
Z | HOH836 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG X 165 |
Chain | Residue |
X | HOH828 |
X | HOH990 |
Z | DUP777 |
Z | HOH839 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG Y 165 |
Chain | Residue |
X | DUP777 |
X | HOH920 |
X | HOH993 |
Y | HOH852 |
site_id | AC8 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE DUP B 777 |
Chain | Residue |
A | ALA98 |
A | GLY99 |
A | VAL100 |
A | ILE101 |
A | ASP102 |
A | TYR105 |
A | GLY110 |
A | HOH779 |
B | ARG153 |
B | GLY157 |
B | PHE158 |
B | GLY159 |
B | SER160 |
B | THR161 |
B | HOH779 |
B | HOH780 |
B | HOH849 |
C | ARG85 |
C | SER86 |
C | GLY87 |
C | GLN131 |
C | MG778 |
C | HOH855 |
X | HOH784 |
X | HOH874 |
site_id | AC9 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE DUP A 777 |
Chain | Residue |
A | ARG153 |
A | GLY157 |
A | PHE158 |
A | GLY159 |
A | SER160 |
A | THR161 |
A | HOH783 |
B | ARG85 |
B | SER86 |
B | GLY87 |
B | GLN131 |
B | MG165 |
B | HOH796 |
B | HOH856 |
C | ALA98 |
C | GLY99 |
C | VAL100 |
C | ILE101 |
C | ASP102 |
C | TYR105 |
C | GLY110 |
X | HOH786 |
X | HOH799 |
X | HOH800 |
X | HOH888 |
site_id | BC1 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE DUP Y 777 |
Chain | Residue |
X | ALA98 |
X | GLY99 |
X | VAL100 |
X | ILE101 |
X | ASP102 |
X | TYR105 |
X | ASN108 |
X | GLY110 |
X | HOH796 |
X | HOH849 |
X | HOH868 |
Y | ARG153 |
Y | GLY157 |
Y | PHE158 |
Y | GLY159 |
Y | SER160 |
Y | THR161 |
Y | HOH780 |
Y | HOH854 |
Z | ARG85 |
Z | SER86 |
Z | GLY87 |
Z | GLN131 |
Z | MG165 |
Z | HOH779 |
Z | HOH836 |
site_id | BC2 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE DUP Z 777 |
Chain | Residue |
X | ARG85 |
X | SER86 |
X | GLY87 |
X | GLN131 |
X | MG165 |
X | HOH788 |
X | HOH828 |
X | HOH990 |
Y | ALA98 |
Y | GLY99 |
Y | VAL100 |
Y | ILE101 |
Y | ASP102 |
Y | TYR105 |
Y | GLY110 |
Y | HOH778 |
Z | ARG153 |
Z | GLY157 |
Z | PHE158 |
Z | GLY159 |
Z | SER160 |
Z | THR161 |
Z | HOH781 |
Z | HOH782 |
Z | HOH839 |
site_id | BC3 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE DUP X 777 |
Chain | Residue |
X | ARG153 |
X | GLY157 |
X | PHE158 |
X | GLY159 |
X | SER160 |
X | THR161 |
X | HOH779 |
X | HOH783 |
X | HOH831 |
X | HOH920 |
X | HOH993 |
Y | ARG85 |
Y | SER86 |
Y | GLY87 |
Y | GLN131 |
Y | MG165 |
Y | HOH852 |
Z | ALA98 |
Z | GLY99 |
Z | VAL100 |
Z | ILE101 |
Z | ASP102 |
Z | TYR105 |
Z | GLY110 |
Z | HOH778 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG X 778 |
Chain | Residue |
X | ASP95 |
X | HOH953 |
X | HOH960 |
X | HOH994 |
Y | ASP95 |
Y | HOH824 |
Z | ASP95 |
site_id | BC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG A 778 |
Chain | Residue |
A | ASP95 |
A | HOH839 |
A | HOH852 |
B | ASP95 |
B | HOH803 |
B | HOH883 |
C | ASP95 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8805593, ECO:0000305|PubMed:17880943, ECO:0007744|PDB:1Q5H, ECO:0007744|PDB:2HQU, ECO:0007744|PDB:3EHW |
Chain | Residue | Details |
A | ARG85 | |
X | ARG85 | |
X | ARG153 | |
X | PHE158 | |
Y | ARG85 | |
Y | ARG153 | |
Y | PHE158 | |
Z | ARG85 | |
Z | ARG153 | |
Z | PHE158 | |
A | ARG153 | |
A | PHE158 | |
B | ARG85 | |
B | ARG153 | |
B | PHE158 | |
C | ARG85 | |
C | ARG153 | |
C | PHE158 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8805593, ECO:0000305|PubMed:17880943, ECO:0007744|PDB:1Q5H, ECO:0007744|PDB:2HQU, ECO:0007744|PDB:3ARA, ECO:0007744|PDB:3ARN, ECO:0007744|PDB:3EHW |
Chain | Residue | Details |
A | GLY99 | |
Y | GLY110 | |
Z | GLY99 | |
Z | GLY110 | |
A | GLY110 | |
B | GLY99 | |
B | GLY110 | |
C | GLY99 | |
C | GLY110 | |
X | GLY99 | |
X | GLY110 | |
Y | GLY99 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | LEU88 | |
B | LEU88 | |
C | LEU88 | |
X | LEU88 | |
Y | LEU88 | |
Z | LEU88 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | GLY99 | |
B | GLY99 | |
C | GLY99 | |
X | GLY99 | |
Y | GLY99 | |
Z | GLY99 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dup |
Chain | Residue | Details |
A | ASP102 | |
A | ASP104 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dup |
Chain | Residue | Details |
B | ASP102 | |
B | ASP104 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dup |
Chain | Residue | Details |
C | ASP102 | |
C | ASP104 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dup |
Chain | Residue | Details |
X | ASP102 | |
X | ASP104 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dup |
Chain | Residue | Details |
Y | ASP102 | |
Y | ASP104 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dup |
Chain | Residue | Details |
Z | ASP102 | |
Z | ASP104 |