Research workbench
Solution structure of N-terminal domain of human TIG3 in 2 M urea
Analyse Solution structure of N-terminal domain of human TIG3 in 2 M urea in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LKT
- Type
- protein
- Length
- 125 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Retinoic acid receptor responder protein 3
- EC
- 3.1.1.-
- UniProt
- Q9UL19
- Pockets
- 1 · best druggability 0.30
Structure
solution nmr · 1 distinct chain · 27% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Retinoic acid receptor responder protein 3 (EC 3.1.1.-) | protein | 125 | 27% helix, 28% strand | Q9UL19 |
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 | 70 | 0.30 | 0.74 | 18 | empty |
Compared structures
- 2LKT · Solution structure of N-terminal domain of human TIG3 in 2 M UREA · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UL19 · AlphaFold monomer V2.0 prediction for phospholipase a and acyltransferase 4 (Q9UL19) · a predicted model of the same protein · chain A against A, TM-score 0.71
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 Q9UL19
- Elsewhere: RCSB PDB 2LKT · PDBe 2LKT · UniProt Q9UL19
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