4KYC
Structure of the C-terminal domain of the Menangle virus phosphoprotein, fused to MBP.
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | Maltose-binding periplasmic protein, Phosphoprotein, chimeric construct | polymer | 420 | 46117.4 | 1 | UniProt (P0AEX9) UniProt (Q91MK1) Pfam (PF01547) | Escherichia coli | MBP, MMBP, Maltodextrin-binding protein |
| 2 | B (B) | alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose | branched | 342.3 | 1 | In PDB BIRD (PRD_900001) GlyTouCan (G07411ON) | alpha-maltose | ||
| 3 | C (A) | 1,2-ETHANEDIOL | non-polymer | 62.1 | 1 | Chemie (EDO) | |||
| 4 | D (A) | BORIC ACID | non-polymer | 61.8 | 1 | Chemie (BO3) | |||
| 5 | E (A) | water | water | 18.0 | 300 | Chemie (HOH) |
Sequence modifications
A: 1 - 366 (UniProt: P0AEX9)
A: 1339 - 1388 (UniProt: Q91MK1)
| PDB | External Database | Details |
|---|---|---|
| Ala 172 | Glu 198 | engineered mutation |
| Ala 173 | Asn 199 | engineered mutation |
| Ala 359 | Glu 385 | engineered mutation |
| Ala 362 | Lys 388 | engineered mutation |
| Ala 363 | Asp 389 | engineered mutation |
| Asn 367 | - | linker |
| Ala 368 | - | linker |
| Ala 369 | - | linker |
| Ala 370 | - | linker |
| PDB | External Database | Details |
|---|---|---|
| Ser 1352 | Cys 352 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 46117.4 | |
| Branched | Number of molecules | 1 |
| Total formula weight | 342.3 | |
| Non-Polymers* | Number of molecules | 2 |
| Total formula weight | 123.9 | |
| All* | Total formula weight | 46583.6 |
