4F5H
Intercoversion of Substrate Specificity: E. coli Aspatate Aminotransferase to Tyrosine Aminotransferase: Chimera P3.
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A, B (A, B) | Aspartate aminotransferase | polymer | 406 | 44845.4 | 2 | UniProt (P00509) Pfam (PF00155) | Escherichia coli | AspAT, Transaminase A |
2 | C, D (A, B) | water | water | 18.0 | 968 | 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 |
Met 56 | Leu 46 | 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 |
Gly 228 | Ala 218 | ENGINEERED MUTATION |
Ser 295 | Asn 285 | ENGINEERED MUTATION |
Leu 331 | Met 321 | ENGINEERED MUTATION |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 2 |
Total formula weight | 89690.8 | |
All* | Total formula weight | 89690.8 |