Crystallization (Comment) | Organism |
---|---|
in complex with its endogenous inhibitor LDI, at 2.7 A resolution. A hydrophobic cluster flanked by ionic interactions in the protein-protein interface is vital for the picomolar affinity of LDI to the enzyme | Hordeum vulgare |
Protein Variants | Comment | Organism |
---|---|---|
D730R | modest change in the association rate constant with endogenous inhibitor LDI. Residue D730 binds in a positively charged pocket on the surface of LDI via a hydrogen bond and a salt bridge to residue Arg34 and a hydrogen bond to Arg84 of LDI. D730 adopts different rotamers in the free enzyme and enzyme bound to LDI | Hordeum vulgare |
D730W | modest change in the association rate constant with endogenous inhibitor LDI. Residue D730 binds in a positively charged pocket on the surface of LDI via a hydrogen bond and a salt bridge to residue Arg34 and a hydrogen bond to Arg84 of LDI. D730 adopts different rotamers in the free enzyme and enzyme bound to LDI | Hordeum vulgare |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Hordeum vulgare | O48541 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
HvLD99 | - |
Hordeum vulgare |