Research workbench
Triosephosphate isomerase of synechocystis in complex with 2- phosphoglycolic acid
Analyse Triosephosphate isomerase of synechocystis in complex with 2- phosphoglycolic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BVE
- Type
- protein
- Length
- 484 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triosephosphate isomerase
- EC
- 5.3.1.1
- UniProt
- Q59994
- Ligands
- PGA, NA
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Triosephosphate isomerase (EC 5.3.1.1) | protein | 242 | 42% helix, 16% strand | Q59994 |
Ligands and binding sites
- PGA · 2-phosphoglycolic acid · ligand · 2 copies · chains A, B
- NA · Sodium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1740 Ų buried · 33 hydrogen bonds · protein-protein
Compared structures
- 6BVE · Triosephosphate isomerase of Synechocystis in complex with 2-Phosphoglycolic acid · the same entry in another collection · chain A against A, TM-score 1.00
- Q59994 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase (Q59994) · 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 Q59994
- Elsewhere: RCSB PDB 6BVE · PDBe 6BVE · UniProt Q59994
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.