| Region 1 |
| Type: | Disordered |
| Name: | |
| Location: | 57 - 64 |
| Length: | 8 |
| Region sequence: |
PLADGPTI |
| Modification type: | |
| PDB: | |
| Structural/functional type: | Function arises via an order to disorder transition
|
| Functional classes: | Molecular assembly
|
| Functional subclasses: | Protein-protein binding
|
Detection methods:
- X-ray crystallography (288 K; ammonium sulfate 1.8 M; potassium phosphate (buffer (pH 7.0)) 5 mM; protein (solution (20 mg/mL)) 1 uL; sodium cacodylate (pH 6.5) 0.1 M)
|
References:
- Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K. "Conformational changes in the alpha-subunit coupled to binding of the beta 2-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase alpha-subunit alone." Biochemistry. 2005; 44(4): 1184-92. PubMed: 15667212
|
Comments:These densities were unclear in molecule A only. The region stayed disordered when in a complex with molecule B.
|
| Region 2 |
| Type: | Disordered |
| Name: | |
| Location: | 184 - 185 |
| Length: | 2 |
| Region sequence: |
GA |
| Modification type: | |
| PDB: | |
| Structural/functional type: | Relationship to function unknown
|
| Functional classes: | Unknown
|
| Functional subclasses: | Unknown
|
Detection methods:
- X-ray crystallography (288 K; ammonium sulfate 1.8 M; potassium phosphate (buffer (pH 7.0)) 5 mM; protein (solution (20 mg/mL)) 1 uL; sodium cacodylate (pH 6.5) 0.1 M)
|
References:
- Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K. "Conformational changes in the alpha-subunit coupled to binding of the beta 2-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase alpha-subunit alone." Biochemistry. 2005; 44(4): 1184-92. PubMed: 15667212
|
Comments:These densities were unclear in molecules A and B.
|
| Region 3 |
| Type: | Disordered |
| Name: | |
| Location: | 59 - 63 |
| Length: | 5 |
| Region sequence: |
ADGPT |
| Modification type: | |
| PDB: | |
| Structural/functional type: | Function arises via an order to disorder transition
|
| Functional classes: | Molecular assembly
|
| Functional subclasses: | Protein-protein binding
|
Detection methods:
- X-ray crystallography (288 K; ammonium sulfate 1.8 M; potassium phosphate (buffer (pH 7.0)) 5 mM; protein (solution (20 mg/mL)) 1 uL; sodium cacodylate (pH 6.5) 0.1 M)
|
References:
- Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K. "Conformational changes in the alpha-subunit coupled to binding of the beta 2-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase alpha-subunit alone." Biochemistry. 2005; 44(4): 1184-92. PubMed: 15667212
|
Comments:These densities are unclear in molecule B only. The region stayed disordered when in complex with molecule A.
|
