4F5J
Rational Design and Directed Evolution for Conversion of Substrate Specificity from E.coli Aspartate Aminotransferase to Tyrosine Aminotransferase: Mutant P5.
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A, B | Aspartate aminotransferase | polymer | 406 | 44764.3 | 2 | UniProt (P00509) Pfam (PF00155) In PDB | Escherichia coli | AspAT, Transaminase A |
2 | water | water | 18.0 | 942 | Chemie (HOH) |
Sequence modifications
A, B: 12 - 406 (UniProt: P00509)
PDB | External Database | Details |
---|---|---|
Met 1 | - | EXPRESSION TAG |
Ala 2 | - | EXPRESSION TAG |
His 3 | - | EXPRESSION TAG |
His 4 | - | EXPRESSION TAG |
His 5 | - | EXPRESSION TAG |
His 6 | - | EXPRESSION TAG |
His 7 | - | EXPRESSION TAG |
His 8 | - | EXPRESSION TAG |
Val 9 | - | EXPRESSION TAG |
Gly 10 | - | EXPRESSION TAG |
Thr 11 | - | EXPRESSION TAG |
Val 39 | Ile 29 | ENGINEERED MUTATION |
Asp 40 | Asn 30 | ENGINEERED MUTATION |
Val 43 | Ile 33 | ENGINEERED MUTATION |
Thr 74 | Asn 64 | ENGINEERED MUTATION |
Leu 78 | Ile 68 | ENGINEERED MUTATION |
Leu 81 | Ile 71 | ENGINEERED MUTATION |
Ser 114 | Thr 104 | ENGINEERED MUTATION |
Ala 145 | Ser 135 | ENGINEERED MUTATION |
Ile 146 | Val 136 | ENGINEERED MUTATION |
Ala 197 | Ile 187 | ENGINEERED MUTATION |
Ile 220 | Phe 210 | ENGINEERED MUTATION |
Ile 222 | Phe 212 | ENGINEERED MUTATION |
Gly 228 | Ala 218 | ENGINEERED MUTATION |
Cys 254 | Tyr 244 | ENGINEERED MUTATION |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 2 |
Total formula weight | 89528.7 | |
All* | Total formula weight | 89528.7 |