2QXX
Bifunctional dCTP deaminase: dUTPase from Mycobacterium tuberculosis in complex with dTTP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004170 | molecular_function | dUTP diphosphatase activity |
| 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 | 0015949 | biological_process | nucleobase-containing small molecule interconversion |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0033973 | molecular_function | dCTP deaminase (dUMP-forming) activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004170 | molecular_function | dUTP diphosphatase activity |
| 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 | 0015949 | biological_process | nucleobase-containing small molecule interconversion |
| 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 | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 202 |
| Chain | Residue |
| A | TTP201 |
| A | HOH237 |
| A | HOH239 |
| A | HOH265 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 202 |
| Chain | Residue |
| B | TTP201 |
| B | HOH229 |
| B | HOH247 |
| B | HOH268 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE TTP A 201 |
| Chain | Residue |
| A | SER102 |
| A | SER103 |
| A | ARG106 |
| A | ALA115 |
| A | GLY116 |
| A | PHE117 |
| A | ILE118 |
| A | ASP119 |
| A | ILE126 |
| A | THR127 |
| A | GLN148 |
| A | TYR162 |
| A | SER169 |
| A | LYS170 |
| A | TYR171 |
| A | GLN174 |
| A | MG202 |
| A | HOH233 |
| A | HOH237 |
| A | HOH239 |
| A | HOH240 |
| A | HOH243 |
| A | HOH265 |
| A | HOH288 |
| A | LYS101 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE 1PE A 203 |
| Chain | Residue |
| A | ARG47 |
| A | TYR48 |
| A | THR49 |
| A | GLN57 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE TTP B 201 |
| Chain | Residue |
| B | LYS101 |
| B | SER102 |
| B | SER103 |
| B | ARG106 |
| B | ALA115 |
| B | GLY116 |
| B | PHE117 |
| B | ASP119 |
| B | ILE126 |
| B | THR127 |
| B | GLN148 |
| B | TYR162 |
| B | SER169 |
| B | LYS170 |
| B | TYR171 |
| B | GLN174 |
| B | MG202 |
| B | HOH228 |
| B | HOH229 |
| B | HOH234 |
| B | HOH235 |
| B | HOH237 |
| B | HOH247 |
| B | HOH268 |
| B | HOH279 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE 1PE B 203 |
| Chain | Residue |
| B | GLY15 |
| B | ARG16 |
| B | THR89 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 1PE B 204 |
| Chain | Residue |
| B | ARG47 |
| B | TYR48 |
| B | THR49 |
| B | GLN57 |
| B | SER165 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P28248","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00146","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00146","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"NOV-2011","submissionDatabase":"PDB data bank","title":"Dttp inhibition of the bifunctional Dctp deaminase- dutpase from Mycobacterium tuberculosis is pH dependent: kinetic analyses and crystal structure of A115V Variant.","authors":["Lovgreen M.N.","Harris P.","Ucar E.","Willemoes M."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00146","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18164314","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"NOV-2011","submissionDatabase":"PDB data bank","title":"Dttp inhibition of the bifunctional Dctp deaminase- dutpase from Mycobacterium tuberculosis is pH dependent: kinetic analyses and crystal structure of A115V Variant.","authors":["Lovgreen M.N.","Harris P.","Ucar E.","Willemoes M."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for bifunctional activity","evidences":[{"source":"HAMAP-Rule","id":"MF_00146","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18164314","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 | GLY121 | |
| A | ASP119 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dup |
| Chain | Residue | Details |
| B | GLY121 | |
| B | ASP119 |
