2J4H
Crystal structure of a H121A Escherichia coli dCTP deaminase mutant enzyme
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005829 | cellular_component | cytosol |
A | 0006226 | biological_process | dUMP biosynthetic process |
A | 0006229 | biological_process | dUTP biosynthetic process |
A | 0006235 | biological_process | dTTP biosynthetic process |
A | 0008829 | molecular_function | dCTP deaminase activity |
A | 0009117 | biological_process | nucleotide metabolic process |
A | 0009314 | biological_process | response to radiation |
A | 0015949 | biological_process | nucleobase-containing small molecule interconversion |
A | 0016787 | molecular_function | hydrolase activity |
A | 0032991 | cellular_component | protein-containing complex |
A | 0042802 | molecular_function | identical protein binding |
A | 0070207 | biological_process | protein homotrimerization |
B | 0000166 | molecular_function | nucleotide binding |
B | 0005829 | cellular_component | cytosol |
B | 0006226 | biological_process | dUMP biosynthetic process |
B | 0006229 | biological_process | dUTP biosynthetic process |
B | 0006235 | biological_process | dTTP biosynthetic process |
B | 0008829 | molecular_function | dCTP deaminase activity |
B | 0009117 | biological_process | nucleotide metabolic process |
B | 0009314 | biological_process | response to radiation |
B | 0015949 | biological_process | nucleobase-containing small molecule interconversion |
B | 0016787 | molecular_function | hydrolase activity |
B | 0032991 | cellular_component | protein-containing complex |
B | 0042802 | molecular_function | identical protein binding |
B | 0070207 | biological_process | protein homotrimerization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE YYY A1175 |
Chain | Residue |
A | GLY109 |
A | TRP131 |
A | ILE135 |
A | VAL136 |
A | GLU138 |
A | MG1176 |
A | ARG110 |
A | SER111 |
A | SER112 |
A | ARG115 |
A | ALA121 |
A | ALA124 |
A | ARG126 |
A | ASP128 |
site_id | AC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MG A1176 |
Chain | Residue |
A | YYY1175 |
site_id | AC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE YYY B1173 |
Chain | Residue |
B | GLY109 |
B | ARG110 |
B | SER111 |
B | SER112 |
B | ARG115 |
B | ALA121 |
B | ALA124 |
B | ARG126 |
B | ASP128 |
B | TRP131 |
B | ILE135 |
B | VAL136 |
B | GLU138 |
B | MG1174 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MG B1174 |
Chain | Residue |
B | YYY1173 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG A1177 |
Chain | Residue |
A | ALA121 |
A | VAL122 |
A | HIS125 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG B1175 |
Chain | Residue |
B | LEU107 |
B | ALA121 |
B | VAL122 |
B | HIS125 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00146, ECO:0000305|PubMed:15539408, ECO:0000305|PubMed:17996716 |
Chain | Residue | Details |
A | GLU138 | |
B | GLU138 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00146, ECO:0000305|PubMed:15539408, ECO:0000305|PubMed:17651436, ECO:0000305|PubMed:17996716 |
Chain | Residue | Details |
A | ARG110 | |
A | VAL136 | |
B | ARG110 | |
B | VAL136 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:15539408, ECO:0000305|PubMed:17651436, ECO:0000305|PubMed:17996716 |
Chain | Residue | Details |
A | ALA124 | |
B | ALA124 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:15539408, ECO:0000305|PubMed:17996716 |
Chain | Residue | Details |
A | TYR171 | |
B | TYR171 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00146, ECO:0000305|PubMed:15539408, ECO:0000305|PubMed:17996716 |
Chain | Residue | Details |
A | LYS178 | |
A | GLN182 | |
B | LYS178 | |
B | GLN182 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dup |
Chain | Residue | Details |
A | GLY130 | |
A | ASP128 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dup |
Chain | Residue | Details |
B | GLY130 | |
B | ASP128 |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 732 |
Chain | Residue | Details |
A | SER111 | electrostatic stabiliser |
A | ARG115 | electrostatic stabiliser |
A | ALA124 | electrostatic stabiliser |
A | ARG126 | steric role |
A | GLU138 | proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 732 |
Chain | Residue | Details |
B | SER111 | electrostatic stabiliser |
B | ARG115 | electrostatic stabiliser |
B | ALA124 | electrostatic stabiliser |
B | ARG126 | steric role |
B | GLU138 | proton acceptor, proton donor |