2GB5
Crystal structure of NADH pyrophosphatase (EC 3.6.1.22) (1790429) from Escherichia coli K12 at 2.30 A resolution
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) | NADH pyrophosphatase | polymer | 269 | 31608.6 | 2 | UniProt (P32664) Pfam (PF09297) Pfam (PF00293) | Escherichia coli | |
| 2 | C, D (A, B) | ZINC ION | non-polymer | 65.4 | 2 | Chemie (ZN) | |||
| 3 | E, F (A, B) | water | water | 18.0 | 240 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 257 (UniProt: P32664)
| PDB | External Database | Details |
|---|---|---|
| Mse -11 | - | expression tag |
| Gly -10 | - | expression tag |
| Ser -9 | - | expression tag |
| Asp -8 | - | expression tag |
| Lys -7 | - | expression tag |
| Ile -6 | - | expression tag |
| His -5 | - | expression tag |
| His -4 | - | expression tag |
| His -3 | - | expression tag |
| His -2 | - | expression tag |
| His -1 | - | expression tag |
| His 0 | - | expression tag |
| Mse 1 | Met 1 | modified residue |
| Mse 65 | Met 65 | modified residue |
| Mse 105 | Met 105 | modified residue |
| Mse 114 | Met 114 | modified residue |
| Mse 176 | Met 176 | modified residue |
| Mse 201 | Met 201 | modified residue |
| Mse 205 | Met 205 | modified residue |
| Mse 251 | Met 251 | modified residue |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 63217.2 | |
| Non-Polymers* | Number of molecules | 2 |
| Total formula weight | 130.8 | |
| All* | Total formula weight | 63348.0 |






