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Crystal structure of rabbit muscle triosephosphate isomerase
Analyse Crystal structure of rabbit muscle triosephosphate isomerase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1R2T
- Type
- protein
- Length
- 493 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triosephosphate isomerase
- EC
- 5.3.1.1
- UniProt
- P00939
- Pockets
- 4 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Triosephosphate isomerase (EC 5.3.1.1) | protein | 246 | 45% helix, 17% strand | P00939 |
| B | Triosephosphate isomerase (EC 5.3.1.1) | protein | 247 | 45% helix, 16% strand | P00939 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 50 | 0.68 | 0.98 | 15 | empty |
| 2 | 116 | 0.45 | 0.78 | 26 | empty |
| 3 | 128 | 0.45 | 0.77 | 31 | empty |
| 4 | 54 | 0.35 | 0.79 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1798 Ų buried · 41 hydrogen bonds · protein-protein
Compared structures
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 P00939
- Elsewhere: RCSB PDB 1R2T · PDBe 1R2T · UniProt P00939
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