Research workbench
Crystal structure of trichomonas vaginalis triosephosphate isomerase ILE45-ala mutant (TVAG_497370)
Analyse Crystal structure of trichomonas vaginalis triosephosphate isomerase ILE45-ala… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4O50
- Type
- protein
- Length
- 252 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triosephosphate isomerase
- EC
- 5.3.1.1
- UniProt
- A2EGX9
- Ligands
- NA
- Pockets
- 2 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Triosephosphate isomerase (EC 5.3.1.1) | protein | 252 | 45% helix, 14% strand | A2EGX9 |
Ligands and binding sites
- NA · Sodium ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 116 | 0.42 | 0.77 | 28 | empty |
| 2 | 80 | 0.37 | 0.76 | 17 | empty |
Compared structures
- 4O50 · Crystal Structure of Trichomonas vaginalis Triosephosphate Isomerase Ile45-Ala mutant… · 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 A2EGX9
- Elsewhere: RCSB PDB 4O50 · PDBe 4O50 · UniProt A2EGX9
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