Cloned (Comment) | Organism |
---|---|
expression of wild-type an dmutant N-terminal nucleotide binding domains in Escherichia coli strain BL21(DE3) | Candida albicans |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required, both Mg2+ coordination and nucleotide binding contribute to the formation of the active site, entry of Mg2+ into the active site causes the first large conformational change that brings Trp326 and Cys193 in close proximity to each other, besides Trp326, typical Glu238 in the Q-loop also participates in coordination of Mg2+ by the N-terminal nucleotide binding domain | Candida albicans |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + xenobiotic/in | Candida albicans | - |
ADP + phosphate + xenobiotic/out | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Candida albicans | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + xenobiotic/in | - |
Candida albicans | ADP + phosphate + xenobiotic/out | - |
? | |
ATP + H2O + xenobiotic/in | the typical Cys193 in Walker A as well as Trp326 and Asp327 in the Walker B of N-terminal nucleotide binding domain of Cdr1p have acquired unique roles in ATP binding and hydrolysis. Asn328 is a gamma-phosphate sensor. ATP docking subsequent to Mg2+ coordination induces further conformational changes, structure analysis, overview | Candida albicans | ADP + phosphate + xenobiotic/out | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Cdr1p | - |
Candida albicans |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Candida albicans |