Research workbench
Structural genomics of caenorhabditis elegans: triose phosphate isomerase
Analyse Structural genomics of caenorhabditis elegans: triose phosphate isomerase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MO0
- Type
- protein
- Length
- 502 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triosephosphate isomerase
- EC
- 5.3.1.1
- UniProt
- Q10657
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Triosephosphate isomerase (EC 5.3.1.1) | protein | 257 | 42% helix, 16% strand | Q10657 |
| B | Triosephosphate isomerase (EC 5.3.1.1) | protein | 245 | 43% helix, 17% strand | Q10657 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains A, B
- ACT · Acetate ion · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 95 | 0.76 | 0.97 | 28 | empty |
| 2 | 55 | 0.38 | 0.81 | 24 | ACT, SO4 |
Interfaces
1 interface between chains.
- A–B · 1624 Ų buried · 25 hydrogen bonds · protein-protein
Compared structures
- 1MO0 · Structural Genomics Of Caenorhabditis Elegans: Triose Phosphate Isomerase · the same entry in another collection · chain A against A, TM-score 1.00
- Q10657 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase (Q10657) · a predicted model of the same protein · chain B 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 Q10657
- Elsewhere: RCSB PDB 1MO0 · PDBe 1MO0 · UniProt Q10657
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