2V2H
The A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase (TIM) induces a more closed conformation of this hinge region in dimeric and monomeric TIM
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 | TRIOSEPHOSPHATE ISOMERASE GLYCOSOMAL | polymer | 242 | 26075.8 | 3 | UniProt (P04789) Pfam (PF00121) In PDB | TRYPANOSOMA BRUCEI BRUCEI | TRIOSEPHOSPHATE ISOMERASE, TIM, TRIOSE-PHOSPHATE ISOMERASE |
2 | A, B, C | 2-PHOSPHOGLYCOLIC ACID | non-polymer | 156.0 | 3 | Chemie (PGA) | |||
3 | A, B, C | CHLORIDE ION | non-polymer | 35.5 | 3 | Chemie (CL) | |||
4 | water | water | 18.0 | 848 | Chemie (HOH) |
Sequence modifications
A, B, C: 15 - 72 (UniProt: P04789)
A, B, C: 80 - 250 (UniProt: P04789)
PDB | External Database | Details |
---|---|---|
Ser 15 | Asn 15 | conflict |
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 |
Ala 72 | Gly 72 | conflict |
PDB | External Database | Details |
---|---|---|
Ala 81 | Pro 81 | conflict |
Ser 82 | Ile 82 | conflict |
Trp 100 | Ala 100 | conflict |
Leu 178 | Ala 178 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 3 |
Total formula weight | 78227.5 | |
Non-Polymers* | Number of molecules | 6 |
Total formula weight | 574.5 | |
All* | Total formula weight | 78801.9 |