5I3I
Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B, C, D | Triosephosphate isomerase, glycosomal | polymer | 250 | 26823.8 | 4 | UniProt (P04789) Pfam (PF00121) In PDB | Trypanosoma brucei brucei | Triose-phosphate isomerase |
| 2 | A, B, C, D | 2-PHOSPHOGLYCOLIC ACID | non-polymer | 156.0 | 4 | Chemie (PGA) | |||
| 3 | water | water | 18.0 | 363 | Chemie (HOH) |
Sequence modifications
A, B, C, D: 1 - 250 (UniProt: P04789)
| PDB | External Database | Details |
|---|---|---|
| Ala 172 | Ile 172 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 4 |
| Total formula weight | 107295.0 | |
| Non-Polymers* | Number of molecules | 4 |
| Total formula weight | 624.1 | |
| All* | Total formula weight | 107919.1 |
