Research workbench
NMR structure of the MDVL1 PDZ domain in complex with its inhibitor
Analyse NMR structure of the MDVL1 PDZ domain in complex with its inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KAW
- Type
- protein
- Length
- 90 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Segment polarity protein dishevelled homolog dvl-1
- UniProt
- P51141
- Ligands
- SUZ
Structure
solution nmr · 1 distinct chain · 13% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Segment polarity protein dishevelled homolog dvl-1 | protein | 90 | 13% helix, 33% strand | P51141 |
Ligands and binding sites
- SUZ · [(1Z)-5-fluoro-2-methyl-1-{4-[methylsulfinyl]benzylidene}-1H-inden-3-yl]acetic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2KAW · NMR structure of the mDvl1 PDZ domain in complex with its inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
- P51141 · AlphaFold monomer V2.0 prediction for segment polarity protein dishevelled homolog dvl-1… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P51141
- Elsewhere: RCSB PDB 2KAW · PDBe 2KAW · UniProt P51141
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