Research workbench
TIM-2
Analyse TIM-2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OR7
- Type
- protein
- Length
- 222 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- T-cell immunoglobulin and mucin domain- containing protein 2
- UniProt
- Q8R183
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 2 distinct chains · 11% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | T-cell immunoglobulin and mucin domain- containing protein 2 | protein | 107 | 13% helix, 42% strand | Q8R183 |
| B | T-cell immunoglobulin and mucin domain- containing protein 2 | protein | 115 | 9% helix, 41% strand | Q8R183 |
Ligands and binding sites
- ACT · Acetate ion · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 113 | 0.39 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 844 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
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 Q8R183
- Elsewhere: RCSB PDB 2OR7 · PDBe 2OR7 · UniProt Q8R183
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