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PDBe Entry: 1pkj 
Structural basis for recognition and catalysis by the bifunctional dCTP deaminase and dUTPase from Methanococcus jannaschii
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HYDROLASE
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X-RAY DIFFRACTION
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Resolution: 2.1 Å, R-factor: 19.3%, Free R-factor: 23.3%, Spacegroup: P 21 3
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23/09/2003, deposition: 05/06/2003, last revision: 24/02/2009
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Huffman, J.L. ; Li, H. ; White, R.H. ; Tainer, J.A.
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Structural basis for recognition and catalysis by the bifunctional dCTP deaminase and dUTPase from Methanococcus jannaschii J.MOL.BIOL. vol:331, pag:885-896 (2003) [PubMed ID 12909016 ]
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DCTP DEAMINASE , DUTPASE , DCD-DUT , MJ0430 , DCTP , DUTP , HYDROLASE
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3.5.4.30 ExPASy BRENDA (A B)
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Methanocaldococcus jannaschii 2190 (A B)
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dCTP deaminase, dUMP-forming (EC 3.5.4.30) (Bifunctional deaminase/diphosphatase) (MjDCD-DUT) (DCD/DUT) Q57872 (A B)
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A, B
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1pkh, 1pkk
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| A, B |
Bifunctional deaminase/diphosphatase |
Protein |
Q57872 (DCD_METJA)
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204 |
88% |
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| B |
DEOXYURIDINE-5'-TRIPHOSPHATE |
DUT
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| A, B |
1,2-ETHANEDIOL |
EDO
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