3A6V
Crystal structure of the MutT protein in MN(II) bound holo form
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0005515 | molecular_function | protein binding |
A | 0006203 | biological_process | dGTP catabolic process |
A | 0006260 | biological_process | DNA replication |
A | 0006281 | biological_process | DNA repair |
A | 0006289 | biological_process | nucleotide-excision repair |
A | 0006974 | biological_process | DNA damage response |
A | 0008413 | molecular_function | 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0030145 | molecular_function | manganese ion binding |
A | 0035539 | molecular_function | 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity |
A | 0044715 | molecular_function | 8-oxo-dGDP phosphatase activity |
A | 0044716 | molecular_function | 8-oxo-GDP phosphatase activity |
A | 0046067 | biological_process | dGDP catabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0047693 | molecular_function | ATP diphosphatase activity |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0005515 | molecular_function | protein binding |
B | 0006203 | biological_process | dGTP catabolic process |
B | 0006260 | biological_process | DNA replication |
B | 0006281 | biological_process | DNA repair |
B | 0006289 | biological_process | nucleotide-excision repair |
B | 0006974 | biological_process | DNA damage response |
B | 0008413 | molecular_function | 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0030145 | molecular_function | manganese ion binding |
B | 0035539 | molecular_function | 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity |
B | 0044715 | molecular_function | 8-oxo-dGDP phosphatase activity |
B | 0044716 | molecular_function | 8-oxo-GDP phosphatase activity |
B | 0046067 | biological_process | dGDP catabolic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0047693 | molecular_function | ATP diphosphatase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 1003 |
Chain | Residue |
A | GLU53 |
A | GLU57 |
A | HOH132 |
A | HOH133 |
B | ASP77 |
B | HOH132 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 1004 |
Chain | Residue |
B | HOH132 |
B | HOH138 |
B | TLA2001 |
A | GLU53 |
A | HOH131 |
A | HOH134 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 1005 |
Chain | Residue |
A | GLY37 |
A | GLU57 |
A | HOH153 |
B | ASP77 |
B | HOH186 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE TLA A 2002 |
Chain | Residue |
A | LYS39 |
A | ARG78 |
A | HOH149 |
B | LYS39 |
B | ARG78 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE TLA A 2003 |
Chain | Residue |
A | LYS2 |
A | ARG78 |
A | HOH138 |
B | GLU41 |
B | HOH134 |
B | HOH135 |
B | HOH150 |
B | MN1002 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 1001 |
Chain | Residue |
A | ASP77 |
A | HOH136 |
B | GLU53 |
B | GLU57 |
B | HOH137 |
B | HOH181 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 1002 |
Chain | Residue |
A | HOH136 |
A | HOH138 |
A | TLA2003 |
B | GLU53 |
B | HOH134 |
B | HOH135 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA B 1006 |
Chain | Residue |
A | ASP77 |
A | HOH163 |
B | GLY37 |
B | GLU57 |
B | HOH140 |
site_id | AC9 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE TLA B 2001 |
Chain | Residue |
A | GLU41 |
A | HOH131 |
A | HOH134 |
A | HOH158 |
A | HOH191 |
A | MN1004 |
B | LYS2 |
B | ARG78 |
B | HOH132 |
B | HOH138 |
B | HOH142 |
Functional Information from PROSITE/UniProt
site_id | PS00893 |
Number of Residues | 22 |
Details | NUDIX_BOX Nudix box signature. GkiemgEtpeqAVvRELqEEvG |
Chain | Residue | Details |
A | GLY38-GLY59 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000305|PubMed:19864691 |
Chain | Residue | Details |
A | ARG23 | |
A | HIS28 | |
A | GLU34 | |
B | ARG23 | |
B | HIS28 | |
B | GLU34 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19864691 |
Chain | Residue | Details |
A | GLY37 | |
A | GLU57 | |
B | GLY37 | |
B | GLU57 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:12939141, ECO:0000305|PubMed:19864691 |
Chain | Residue | Details |
A | ASN119 | |
B | ASN119 |