6V9K
CRYSTAL STRUCTURE OF THE HYBRID C-TERMINAL DOMAIN OF ENZYME I OF THE BACTERIAL PHOSPHOTRANSFERASE SYSTEM FORMED BY HYBRIDIZING THE SCAFFOLD OF THE ESCHERICHIA COLI ENZYME WITH THE ACTIVE SITE LOOPS FROM THE THERMOANAEROBACTER TENGCONGENSIS ENZYME
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A, B | Phosphoenolpyruvate-protein phosphotransferase | polymer | 316 | 35468.7 | 2 | UniProt (A0A4S4CN20) Pfam (PF02896) UniProt (by SIFTS) (P08839) In PDB | Escherichia coli | Phosphotransferase system,enzyme I |
2 | A, B | MAGNESIUM ION | non-polymer | 24.3 | 2 | Chemie (MG) | |||
3 | water | water | 18.0 | 578 | Chemie (HOH) |
Sequence modifications
A, B: 261 - 575 (UniProt: A0A4S4CN20)
PDB | External Database | Details |
---|---|---|
Met 260 | - | initiating methionine |
Pro 278 | Val 253 | engineered mutation |
Lys 279 | Arg 254 | engineered mutation |
Tyr 301 | Phe 276 | engineered mutation |
Asn 305 | Asp 280 | engineered mutation |
Ser 306 | Ala 281 | engineered mutation |
Ser 309 | Thr 284 | engineered mutation |
Leu 334 | Met 309 | engineered mutation |
Leu 345 | Met 320 | engineered mutation |
Asp 346 | Asn 321 | engineered mutation |
Met 347 | Phe 322 | engineered mutation |
Met 351 | Glu 326 | engineered mutation |
Tyr 357 | Trp 332 | engineered mutation |
Met 466 | Gly 441 | engineered mutation |
Glu 468 | Asp 443 | engineered mutation |
His 469 | Met 444 | engineered mutation |
Val 470 | Ile 445 | engineered mutation |
Lys 471 | Ser 446 | engineered mutation |
Glu 472 | His 447 | engineered mutation |
Tyr 473 | Leu 448 | engineered mutation |
Phe 477 | Met 452 | engineered mutation |
His 478 | Ser 453 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 2 |
Total formula weight | 70937.4 | |
Non-Polymers* | Number of molecules | 2 |
Total formula weight | 48.6 | |
All* | Total formula weight | 70986.0 |