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 | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00146","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15539408","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17996716","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00146","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15539408","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17651436","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17996716","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15539408","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17651436","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17996716","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15539408","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17996716","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
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 |
