2AZD
X-Ray studies on Maltodextrin Phosphorylase (MalP) Complexes: recognition of substrates and CATALYTIC mechanism of phosphorylase family
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B (A, B) | Maltodextrin phosphorylase | polymer | 796 | 90547.1 | 2 | UniProt (P00490) Pfam (PF00343) | Escherichia coli | |
| 2 | C, D (C, D) | alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose | branched | 666.6 | 2 | In PDB GlyTouCan (G69211UR) | |||
| 3 | E, H (A, B) | VANADATE ION | non-polymer | 114.9 | 2 | Chemie (VO4) | |||
| 4 | F, I (A, B) | PYRIDOXAL-5'-PHOSPHATE | non-polymer | 247.1 | 2 | Chemie (PLP) | |||
| 5 | G, J (A, B) | 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL | non-polymer | 122.1 | 2 | Chemie (TRS) | |||
| 6 | K, L (A, B) | water | water | 18.0 | 632 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 796 (UniProt: P00490)
| PDB | External Database | Details |
|---|---|---|
| Ala 261 | His 261 | engineered mutation |
| Phe 262 | Thr 262 | engineered mutation |
| Glu 263 | Ala 263 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 181094.1 | |
| Branched | Number of molecules | 2 |
| Total formula weight | 1333.2 | |
| Non-Polymers* | Number of molecules | 6 |
| Total formula weight | 968.4 | |
| All* | Total formula weight | 183395.7 |
