4LNL
Structure of Escherichia coli Threonine Aldolase in Complex with Allo-Thr
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A, B | Low-specificity L-threonine aldolase | polymer | 333 | 36528.8 | 2 | UniProt (E7U392) In PDB | Escherichia coli | |
2 | A, B | MAGNESIUM ION | non-polymer | 24.3 | 3 | Chemie (MG) | |||
3 | A | N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-threonine | non-polymer | 350.3 | 1 | Chemie (2BO) | |||
4 | A | N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-allothreonine | non-polymer | 350.3 | 1 | Chemie (2BK) | |||
5 | A, B | 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID | non-polymer | 238.3 | 2 | Chemie (EPE) | |||
6 | A | CHLORIDE ION | non-polymer | 35.5 | 1 | Chemie (CL) | |||
7 | B | N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE] | non-polymer | 306.2 | 1 | Chemie (PLG) | |||
8 | water | water | 18.0 | 466 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 333 (UniProt: E7U392)
PDB | External Database | Details |
---|---|---|
Thr 256 | Ala 256 | conflict |
Ala 257 | Thr 257 | conflict |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 2 |
Total formula weight | 73057.5 | |
Non-Polymers* | Number of molecules | 9 |
Total formula weight | 1591.7 | |
All* | Total formula weight | 74649.2 |