3MBQ
Crystal structure of deoxyuridine 5-triphosphate nucleotidohydrolase from Brucella melitensis, orthorhombic crystal form
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 | 0009117 | biological_process | nucleotide metabolic process |
A | 0016787 | molecular_function | hydrolase 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 | 0006226 | biological_process | dUMP biosynthetic process |
B | 0009117 | biological_process | nucleotide metabolic process |
B | 0016787 | molecular_function | hydrolase 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 | 0006226 | biological_process | dUMP biosynthetic process |
C | 0009117 | biological_process | nucleotide metabolic process |
C | 0016787 | molecular_function | hydrolase 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 | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 201 |
Chain | Residue |
A | ARG54 |
B | GLY110 |
B | ASP111 |
B | ASP112 |
B | HOH158 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 203 |
Chain | Residue |
A | ARG38 |
A | ARG121 |
A | HOH158 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 C 201 |
Chain | Residue |
B | HOH243 |
C | LYS82 |
C | GLY110 |
C | ASP111 |
C | ASP112 |
C | HOH225 |
B | ARG54 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 201 |
Chain | Residue |
A | LYS82 |
A | GLY110 |
A | ASP111 |
A | ASP112 |
C | ARG54 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 C 203 |
Chain | Residue |
C | ARG38 |
C | ARG121 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 206 |
Chain | Residue |
C | ARG138 |
C | ALA139 |
C | LYS140 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 200 |
Chain | Residue |
A | ASP23 |
A | ASP36 |
A | LEU37 |
A | ARG38 |
A | HOH207 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 202 |
Chain | Residue |
A | ARG76 |
A | SER77 |
A | GLY78 |
A | ARG121 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 205 |
Chain | Residue |
A | ILE73 |
A | CYS87 |
A | ASN89 |
A | LYS103 |
A | VAL104 |
A | LEU105 |
C | PHE151 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 200 |
Chain | Residue |
B | ASP23 |
B | ASP36 |
B | LEU37 |
B | ARG38 |
B | HOH173 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 202 |
Chain | Residue |
B | ARG76 |
B | SER77 |
B | GLY78 |
B | GLN124 |
B | HOH326 |
B | HOH329 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B 205 |
Chain | Residue |
B | ILE73 |
B | CYS87 |
B | ASN89 |
B | LYS103 |
B | VAL104 |
B | LEU105 |
B | HOH246 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO C 205 |
Chain | Residue |
C | ILE73 |
C | CYS87 |
C | ASN89 |
C | LYS103 |
C | VAL104 |
C | LEU105 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 204 |
Chain | Residue |
A | LEU16 |
A | GLU17 |
A | HIS18 |
site_id | BC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 202 |
Chain | Residue |
C | ARG76 |
C | SER77 |
C | GLY78 |
C | GLN124 |
C | HOH217 |
C | HOH318 |
C | HOH319 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00116 |
Chain | Residue | Details |
A | ARG76 | |
C | ASN89 | |
C | THR93 | |
C | LYS103 | |
A | ASN89 | |
A | THR93 | |
A | LYS103 | |
B | ARG76 | |
B | ASN89 | |
B | THR93 | |
B | LYS103 | |
C | ARG76 |