EC Number   |
|---|
   7.1.1.1 | - |
| 7.1.1.1 | (dI.Q132N)2dIII trimer |
| 7.1.1.1 | 2.2 A crystal structure of the transmembrane domain at pH 6.5. Presence of transient water flows across a narrow pore and a hydrophobic region in the middle of the membrane channel with key residues His42alpha2 (chain A) being protonated and Thr214beta (chain B) displaying a conformational change, respectively, to gate the channel access to both cytoplasmic and periplasmic chambers |
| 7.1.1.1 | cryo-electron microscopy structure in different conformational states. The NADP(H)-binding domain opens the proton channel to the opposite sides of the membrane |
| 7.1.1.1 | crystal structure of domain I i.e. alpha1 subunit, with and without bound NADH, 1.8 A resolution without NADH, 1.9 A with NADH bound |
| 7.1.1.1 | crystal structure of domainI/domain III complex |
| 7.1.1.1 | dI2dIII complex with bound NAD+ and NADP+, NADH and NADPH, and ADP-ribose and NADPH |
| 7.1.1.1 | dI2dIII1 complex with bound NAD+ and 1,4,5,6-tetrahydronicotinamide adenine dinucleotide phosphate the dI2dIII1 complex with bound ,4,5,6-tetrahydronicotinamide adenine dinucleotide and NADP+. dI is the NAD(H)-binding component of transhydrogenase. dIII is the NADP(H)-binding component |
| 7.1.1.1 | dIII domain in the presence of NADPH |
| 7.1.1.1 | dimers of dI domains using hanging-drop vapor diffusion method |
