Research workbench
YAP65 ww domain complexed to acetyl-plppy
Analyse YAP65 ww domain complexed to acetyl-plppy in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1K9R
- Type
- protein
- Length
- 45 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 65 kda yes-associated protein; Ww domain binding protein-1
- UniProt
- P46937
- Ligands
- ACE
Structure
solution nmr · 2 distinct chains · 0% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 65 kda yes-associated protein | protein | 40 | 0% helix, 38% strand | P46937 |
| B | Ww domain binding protein-1 | protein | 5 | 0% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 306 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
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 P46937
- Elsewhere: RCSB PDB 1K9R · PDBe 1K9R · UniProt P46937
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