1PKH
STRUCTURAL BASIS FOR RECOGNITION AND CATALYSIS BY THE BIFUNCTIONAL DCTP DEAMINASE AND DUTPASE FROM METHANOCOCCUS JANNASCHII
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0006226 | biological_process | dUMP biosynthetic process |
A | 0006229 | biological_process | dUTP biosynthetic process |
A | 0008829 | molecular_function | dCTP deaminase activity |
A | 0009117 | biological_process | nucleotide metabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0033973 | molecular_function | dCTP deaminase (dUMP-forming) activity |
B | 0000166 | molecular_function | nucleotide binding |
B | 0006226 | biological_process | dUMP biosynthetic process |
B | 0006229 | biological_process | dUTP biosynthetic process |
B | 0008829 | molecular_function | dCTP deaminase activity |
B | 0009117 | biological_process | nucleotide metabolic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0033973 | molecular_function | dCTP deaminase (dUMP-forming) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 205 |
Chain | Residue |
A | LYS139 |
B | GLU76 |
B | ILE79 |
B | ASN80 |
B | LYS83 |
B | HOH415 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 206 |
Chain | Residue |
B | GLY28 |
B | ASP33 |
B | ARG160 |
B | ASP25 |
B | PHE26 |
B | VAL27 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 205 |
Chain | Residue |
A | ASP25 |
A | PHE26 |
A | VAL27 |
A | ASP33 |
A | ARG160 |
B | ASN87 |
B | HOH504 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 207 |
Chain | Residue |
B | GLU39 |
B | ILE41 |
B | LEU97 |
B | GLY98 |
B | THR99 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 206 |
Chain | Residue |
A | ASP174 |
A | TYR177 |
A | SER178 |
A | HOH433 |
B | LYS60 |
B | LYS62 |
B | HOH338 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 208 |
Chain | Residue |
B | ARG16 |
B | GLU105 |
B | LEU106 |
B | PRO107 |
B | HOH286 |
B | HOH453 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 207 |
Chain | Residue |
A | PRO21 |
A | ASN23 |
A | THR35 |
A | GLU102 |
A | HOH404 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 209 |
Chain | Residue |
B | GLY37 |
B | ASP38 |
B | ASN101 |
B | LYS157 |
B | ASN158 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO B 210 |
Chain | Residue |
B | THR35 |
B | HOH501 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P28248, ECO:0000255|HAMAP-Rule:MF_00146 |
Chain | Residue | Details |
A | GLU145 | |
B | GLU145 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00146 |
Chain | Residue | Details |
B | ARG117 | |
B | GLN163 | |
A | ARG117 | |
A | GLN163 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:12909016 |
Chain | Residue | Details |
A | HIS128 | |
B | HIS128 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|Ref.6 |
Chain | Residue | Details |
A | GLY132 | |
B | GLY132 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00146, ECO:0000305|Ref.6 |
Chain | Residue | Details |
A | LYS184 | |
A | GLN188 | |
B | ASP135 | |
B | TYR177 | |
B | LYS184 | |
B | GLN188 | |
A | ASP135 | |
A | TYR177 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00146, ECO:0000305|PubMed:12909016, ECO:0000305|Ref.6 |
Chain | Residue | Details |
A | THR143 | |
B | THR143 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | SITE: Important for bifunctional activity => ECO:0000255|HAMAP-Rule:MF_00146 |
Chain | Residue | Details |
A | GLY132 | |
B | GLY132 |