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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
- 1R2S
- Type
- protein
- Length
- 987 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triosephosphate isomerase
- EC
- 5.3.1.1
- UniProt
- P00939
- Pockets
- 8 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D | Triosephosphate isomerase (EC 5.3.1.1) | protein | 247 | 45% helix, 17% strand | P00939 |
| B | Triosephosphate isomerase (EC 5.3.1.1) | protein | 246 | 45% helix, 17% strand | P00939 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 911 | 0.84 | 0.86 | 105 | empty |
| 2 | 60 | 0.69 | 0.96 | 17 | empty |
| 3 | 58 | 0.65 | 0.95 | 15 | empty |
| 4 | 129 | 0.49 | 0.79 | 20 | empty |
| 5 | 185 | 0.48 | 0.76 | 30 | empty |
Interfaces
5 interfaces between chains.
- C–D · 1780 Ų buried · 38 hydrogen bonds · protein-protein
- A–B · 1771 Ų buried · 33 hydrogen bonds · protein-protein
- B–D · 582 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 112 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 63 Ų buried · 1 hydrogen bond · 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 1R2S · PDBe 1R2S · UniProt P00939
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