Research workbench
Crystal structure of triosephosphate isomerase sad deletion mutant from opisthorchis viverrini
Analyse Crystal structure of triosephosphate isomerase sad deletion mutant from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZG4
- Type
- protein
- Length
- 971 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triosephosphate isomerase
- EC
- 5.3.1.1
- UniProt
- A0A074Z863
- Pockets
- 11 · best druggability 0.75
Structure
x-ray diffraction · 4 distinct chains · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Triosephosphate isomerase (EC 5.3.1.1) | protein | 245 | 44% helix, 17% strand | A0A074Z863 |
| B | Triosephosphate isomerase (EC 5.3.1.1) | protein | 243 | 44% helix, 16% strand | A0A074Z863 |
| C | Triosephosphate isomerase (EC 5.3.1.1) | protein | 241 | 43% helix, 16% strand | A0A074Z863 |
| D | Triosephosphate isomerase (EC 5.3.1.1) | protein | 242 | 45% helix, 16% strand | A0A074Z863 |
Pockets
11 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 86 | 0.75 | 0.97 | 26 | empty |
| 2 | 84 | 0.74 | 0.97 | 24 | empty |
| 3 | 197 | 0.48 | 0.75 | 23 | empty |
| 4 | 124 | 0.40 | 0.75 | 25 | empty |
| 5 | 63 | 0.40 | 0.80 | 21 | empty |
Interfaces
3 interfaces between chains.
- C–D · 1670 Ų buried · 27 hydrogen bonds · protein-protein
- A–B · 1646 Ų buried · 25 hydrogen bonds · protein-protein
- B–C · 253 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 5ZG4 · Crystal Structure of Triosephosphate isomerase SAD deletion mutant from Opisthorchis… · the same entry in another collection · 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 A0A074Z863
- Elsewhere: RCSB PDB 5ZG4 · PDBe 5ZG4 · UniProt A0A074Z863
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