9HKF
X-Ray crystal structure of a photoswitchable HaloTag bound to JF635
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B (B, A) | Haloalkane dehalogenase,non-specific serine/threonine protein kinase | polymer | 439 | 50100.9 | 2 | UniProt (P0A3G2) UniProt (A0A453KFI0) | Rhodococcus rhodochrous | |
| 2 | C, J (B, A) | CHLORIDE ION | non-polymer | 35.5 | 2 | Chemie (CL) | |||
| 3 | D, K (B, A) | FLAVIN MONONUCLEOTIDE | non-polymer | 456.3 | 2 | Chemie (FMN) | |||
| 4 | E, L (B, A) | (1E,3S)-1-{10-[2-carboxy-5-({2-[2-(hexyloxy)ethoxy]ethyl}carbamoyl)phenyl]-7-(3-fluoroazetidin-1-yl)-5,5-dimethyldibenz o[b,e]silin-3(5H)-ylidene}-3-fluoroazetidin-1-ium | non-polymer | 704.9 | 2 | Chemie (PUJ) | |||
| 5 | F, G, H, I, M... (B, A) | GLYCEROL | non-polymer | 92.1 | 11 | Chemie (GOL) | |||
| 6 | T, U (B, A) | water | water | 18.0 | 376 | Chemie (HOH) |
Sequence modifications
B, A: 3 - 143 (UniProt: P0A3G2)
B, A: 147 - 282 (UniProt: A0A453KFI0)
B, A: 284 - 430 (UniProt: P0A3G2)
| PDB | External Database | Details |
|---|---|---|
| Gly -1 | - | expression tag |
| Pro 0 | - | expression tag |
| Met 1 | - | expression tag |
| Ala 2 | - | expression tag |
| Val 47 | Leu 47 | engineered mutation |
| Thr 58 | Ser 58 | engineered mutation |
| Gly 78 | Asp 78 | engineered mutation |
| Phe 87 | Tyr 87 | engineered mutation |
| Met 88 | Leu 88 | engineered mutation |
| Phe 128 | Cys 128 | engineered mutation |
| Trp 143 | Glu 143 | engineered mutation |
| PDB | External Database | Details |
|---|---|---|
| Ile 155 | Val 54 | engineered mutation |
| Ala 200 | Asp 99 | engineered mutation |
| Arg 265 | Lys 164 | engineered mutation |
| Pro 283 | - | linker |
| PDB | External Database | Details |
|---|---|---|
| Phe 144 | - | linker |
| Ala 145 | - | linker |
| Gly 146 | - | linker |
| Trp 285 | Ala 145 | engineered mutation |
| Thr 295 | Ala 155 | engineered mutation |
| Lys 300 | Glu 160 | engineered mutation |
| Val 307 | Ala 167 | engineered mutation |
| Thr 312 | Ala 172 | engineered mutation |
| Met 315 | Lys 175 | engineered mutation |
| Gly 316 | Cys 176 | engineered mutation |
| Asn 335 | Lys 195 | engineered mutation |
| Glu 364 | Ala 224 | engineered mutation |
| Asp 367 | Asn 227 | engineered mutation |
| Lys 397 | Glu 257 | engineered mutation |
| Ala 404 | Thr 264 | engineered mutation |
| Asn 412 | His 272 | engineered mutation |
| Leu 413 | Tyr 273 | engineered mutation |
| Ser 431 | - | expression tag |
| Thr 432 | - | expression tag |
| Leu 433 | - | expression tag |
| Glu 434 | - | expression tag |
| Ile 435 | - | expression tag |
| Ser 436 | - | expression tag |
| Gly 437 | - | expression tag |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 100201.9 | |
| Non-Polymers* | Number of molecules | 17 |
| Total formula weight | 3406.4 | |
| All* | Total formula weight | 103608.3 |
