2CGL
Crystal Structure of L-rhamnulose kinase from Escherichia coli in complex with L-fructose, ADP and a modeled ATP gamma phosphate.
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | RHAMNULOKINASE | polymer | 489 | 54423.7 | 1 | UniProt (Q8X899) Pfam (PF00370) Pfam (PF02782) UniProt (by SIFTS) (P32171) | ESCHERICHIA COLI BL21(DE3) | L-RHAMNULOSE KINASE, RHAMNULOSE KINASE |
| 2 | B (A) | beta-L-fructofuranose | non-polymer | 180.2 | 1 | Chemie (LFR) | |||
| 3 | C (A) | ADENOSINE-5'-DIPHOSPHATE | non-polymer | 427.2 | 1 | Chemie (ADP) | |||
| 4 | D (A) | PHOSPHITE ION | non-polymer | 79.0 | 1 | Chemie (PO3) | |||
| 5 | E (A) | water | water | 18.0 | 192 | Chemie (HOH) |
Sequence modifications
A: 1 - 489 (UniProt: Q8X899)
| PDB | External Database | Details |
|---|---|---|
| Ala 69 | Glu 69 | engineered mutation |
| Ala 70 | Glu 70 | engineered mutation |
| Ala 73 | Arg 73 | engineered mutation |
| Ala 320 | Ser 320 | conflict |
| Asp 343 | Glu 343 | conflict |
| Glu 344 | Thr 344 | conflict |
| Mse 356 | Thr 356 | conflict |
| Leu 477 | Arg 477 | conflict |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 54423.7 | |
| Non-Polymers* | Number of molecules | 3 |
| Total formula weight | 686.3 | |
| All* | Total formula weight | 55110.0 |
