7Z16
E. coli C-P lyase bound to PhnK/PhnL dual ABC dimer with AMPPNP and PhnK E171Q mutation
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, E (A, E) | Phosphonate C-P lyase system protein PhnG | polymer | 150 | 16545.7 | 2 | UniProt (A0A7T2N2E5) Pfam (PF06754) UniProt (by SIFTS) (P16685) | Escherichia coli | |
| 2 | B, F (B, F) | Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnH | polymer | 194 | 21045.2 | 2 | UniProt (P16686) Pfam (PF05845) | Escherichia coli | RPnTP synthase subunit PhnH |
| 3 | C, G (C, G) | Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnI | polymer | 354 | 38953.7 | 2 | UniProt (A0A1V3VT92) Pfam (PF05861) UniProt (by SIFTS) (P16687) | Escherichia coli | Carbon-phosphorus lyase complex subunit PhnI |
| 4 | D, H (D, H) | Alpha-D-ribose 1-methylphosphonate 5-phosphate C-P lyase | polymer | 281 | 31893.1 | 2 | UniProt (J7QYU2) Pfam (PF06007) UniProt (by SIFTS) (P16688) | Escherichia coli | PRPn C-P lyase |
| 5 | I, J (I, J) | Putative phosphonates utilization ATP-binding protein PhnK | polymer | 291 | 31994.2 | 2 | UniProt (P16678) Pfam (PF00005) Pfam (PF08352) | Escherichia coli | |
| 6 | K, L (K, L) | Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL | polymer | 226 | 24737.5 | 2 | UniProt (P16679) Pfam (PF00005) | Escherichia coli | RPnTP synthase subunit PhnL |
| 7 | M, N, P, Q (C, D, G, H) | ZINC ION | non-polymer | 65.4 | 4 | Chemie (ZN) | |||
| 8 | O, R (D, H) | PHOSPHATE ION | non-polymer | 95.0 | 2 | Chemie (PO4) | |||
| 9 | S, U (I, J) | MAGNESIUM ION | non-polymer | 24.3 | 2 | Chemie (MG) | |||
| 10 | T, V (I, J) | PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER | non-polymer | 506.2 | 2 | Chemie (ANP) | |||
| 11 | W, X (I, J) | water | water | 18.0 | 6 | Chemie (HOH) |
Sequence modifications
I, J: 1 - 252 (UniProt: P16678)
| PDB | External Database | Details |
|---|---|---|
| Gln 171 | Glu 171 | engineered mutation |
| Glu 253 | - | expression tag |
| Asn 254 | - | expression tag |
| Leu 255 | - | expression tag |
| Tyr 256 | - | expression tag |
| Phe 257 | - | expression tag |
| Gln 258 | - | expression tag |
| Gly 259 | - | expression tag |
| Gln 260 | - | expression tag |
| Phe 261 | - | expression tag |
| Gly 262 | - | expression tag |
| Ser 263 | - | expression tag |
| Trp 264 | - | expression tag |
| Ser 265 | - | expression tag |
| His 266 | - | expression tag |
| Pro 267 | - | expression tag |
| Gln 268 | - | expression tag |
| Phe 269 | - | expression tag |
| Glu 270 | - | expression tag |
| Lys 271 | - | expression tag |
| Gly 272 | - | expression tag |
| Gly 273 | - | expression tag |
| Gly 274 | - | expression tag |
| Ser 275 | - | expression tag |
| Gly 276 | - | expression tag |
| Gly 277 | - | expression tag |
| Gly 278 | - | expression tag |
| Ser 279 | - | expression tag |
| Gly 280 | - | expression tag |
| Gly 281 | - | expression tag |
| Gly 282 | - | expression tag |
| Ser 283 | - | expression tag |
| Trp 284 | - | expression tag |
| Ser 285 | - | expression tag |
| His 286 | - | expression tag |
| Pro 287 | - | expression tag |
| Gln 288 | - | expression tag |
| Phe 289 | - | expression tag |
| Glu 290 | - | expression tag |
| Lys 291 | - | expression tag |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 12 |
| Total formula weight | 330338.7 | |
| Non-Polymers* | Number of molecules | 10 |
| Total formula weight | 1512.6 | |
| All* | Total formula weight | 331851.3 |
