Crystallization (Comment) | Organism |
---|---|
structure of mutant R134K in a transition-state analogue complex. The functional enzyme dimer shows significant structural asymmetry with one monomer in a closed conformation with the active site occupied by the transition-state analogue components craetine, MgADP and nitrate. The other monomer has the two loops that control access to the active site in an open conformation and only MgADP is bound | Oryctolagus cuniculus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | deletion of N-terminal 15 amino acids causes dissociation of the functional homodimer into monomers with reduced catalytic activity | Oryctolagus cuniculus |
P20G | disruption of subunit cohesion, causing dissociation of the functional homodimer into monomers with reduced catalytic activity | Oryctolagus cuniculus |
R134K | highly soluble mutant, crystallization data | Oryctolagus cuniculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | P00563 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
muscle | - |
Oryctolagus cuniculus | - |