4DHK
Crystal structure of a deoxycytidine triphosphate deaminase (dCTP deaminase) from Burkholderia thailandensis
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 | 0015949 | biological_process | nucleobase-containing small molecule interconversion |
| A | 0016787 | molecular_function | hydrolase 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 | 0015949 | biological_process | nucleobase-containing small molecule interconversion |
| B | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 201 |
| Chain | Residue |
| A | VAL65 |
| A | ASP66 |
| A | PHE70 |
| A | ASP71 |
| A | SER74 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 202 |
| Chain | Residue |
| A | PHE78 |
| A | LYS79 |
| A | HOH339 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 203 |
| Chain | Residue |
| B | ASN88 |
| A | ASN88 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 204 |
| Chain | Residue |
| A | ARG100 |
| A | ILE101 |
| A | GLU130 |
| A | GLU132 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 205 |
| Chain | Residue |
| A | THR125 |
| A | PHE127 |
| A | TRP131 |
| A | VAL135 |
| A | THR136 |
| A | HOH365 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 201 |
| Chain | Residue |
| B | VAL65 |
| B | ASP66 |
| B | ASP71 |
| B | SER74 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 202 |
| Chain | Residue |
| B | SER113 |
| B | ALA116 |
| B | ASN123 |
| B | THR125 |
| B | THR136 |
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 |
| Chain | Residue | Details |
| A | GLU138 | |
| B | GLU138 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00146 |
| Chain | Residue | Details |
| A | LYS112 | |
| B | GLN181 | |
| A | THR136 | |
| A | GLN157 | |
| A | TYR171 | |
| A | GLN181 | |
| B | LYS112 | |
| B | THR136 | |
| B | GLN157 | |
| B | TYR171 |
