Research workbench
Crystal structure of arabidopsis thaliana cytosolic triosephosphate isomerase C218K mutant
Analyse Crystal structure of arabidopsis thaliana cytosolic triosephosphate isomerase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NXX
- Type
- protein
- Length
- 500 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triosephosphate isomerase, cytosolic
- EC
- 5.3.1.1
- UniProt
- P48491
- Ligands
- NA
- Pockets
- 3 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Triosephosphate isomerase, cytosolic (EC 5.3.1.1) | protein | 250 | 44% helix, 16% strand | P48491 |
Ligands and binding sites
- NA · Sodium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 149 | 0.45 | 0.76 | 25 | empty |
| 2 | 123 | 0.44 | 0.77 | 26 | empty |
| 3 | 57 | 0.40 | 0.81 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1471 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
- 6NXX · Crystal structure of Arabidopsis thaliana cytosolic triosephosphate isomerase C218K mutant · the same entry in another collection · chain A against A, TM-score 1.00
- P48491 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase, cytosolic (P48491) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P48491
- Elsewhere: RCSB PDB 6NXX · PDBe 6NXX · UniProt P48491
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