Research workbench
The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes
Analyse The adaptability of the active site of trypanosomal triosephosphate isomerase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TIM
- Type
- protein
- Length
- 498 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triosephosphate isomerase
- EC
- 5.3.1.1
- UniProt
- P04789
- Ligands
- G3P
- Pockets
- 5 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Triosephosphate isomerase (EC 5.3.1.1) | protein | 249 | 44% helix, 17% strand | P04789 |
Ligands and binding sites
- G3P · Sn-glycerol-3-phosphate · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 121 | 0.42 | 0.77 | 31 | empty |
| 2 | 63 | 0.39 | 0.80 | 21 | G3P |
| 3 | 66 | 0.31 | 0.75 | 14 | empty |
| 4 | 65 | 0.31 | 0.75 | 15 | empty |
| 5 | 50 | 0.31 | 0.77 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1600 Ų buried · 30 hydrogen bonds · protein-protein
Compared structures
- 6TIM · The adaptability of the active site of trypanosomal triosephosphate isomerase as observed… · the same entry in another collection · chain A against A, TM-score 1.00
- 4TIM · Crystallographic and molecular modeling studies on trypanosomal triosephosphate… · a predicted model of the same protein · chain A against A, TM-score 1.00
- 4TIM · Crystallographic and molecular modeling studies on trypanosomal triosephosphate… · a predicted model of the same protein · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P04789
- Elsewhere: RCSB PDB 6TIM · PDBe 6TIM · UniProt P04789
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