2VEN
Structure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B | GLYCOSOMAL TRIOSEPHOSPHATE ISOMERASE | polymer | 238 | 25659.3 | 2 | UniProt (P04789) Pfam (PF00121) In PDB | TRYPANOSOMA BRUCEI BRUCEI | TRIOSEPHOSPHATE ISOMERASE, TIM, TRIOSE-PHOSPHATE ISOMERASE |
| 2 | B | CITRIC ACID | non-polymer | 192.1 | 1 | Chemie (CIT) | |||
| 3 | water | water | 18.0 | 341 | Chemie (HOH) |
Sequence modifications
A, B: 2 - 250 (UniProt: P04789)
| PDB | External Database | Details |
|---|---|---|
| Ser 15 | Cys 14 | conflict |
| - | Asn 15 | deletion |
| Pro 18 | Gln 18 | conflict |
| Asp 19 | Gln 19 | conflict |
| Gly 68 | Ile 68 | conflict |
| Asn 69 | Ala 69 | conflict |
| Ala 70 | Lys 70 | conflict |
| Asp 71 | Ser 71 | conflict |
| - | Gly 72 | deletion |
| - | Ala 73 | deletion |
| - | Phe 74 | deletion |
| - | Thr 75 | deletion |
| - | Gly 76 | deletion |
| - | Glu 77 | deletion |
| - | Val 78 | deletion |
| Ala 72 | Ser 79 | conflict |
| Ala 81 | Pro 81 | conflict |
| Ser 82 | Ile 82 | conflict |
| Trp 100 | Ala 100 | conflict |
| Ala 233 | Val 233 | engineered mutation |
| - | Gly 235 | deletion |
| - | Ala 236 | deletion |
| - | Ser 237 | deletion |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 51318.6 | |
| Non-Polymers* | Number of molecules | 1 |
| Total formula weight | 192.1 | |
| All* | Total formula weight | 51510.7 |
