Research workbench
Solution structure of the complex between the DDEF1 SH3 domain and the apc SAMP1 motif
Analyse Solution structure of the complex between the DDEF1 SH3 domain and the apc… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RQU
- Type
- protein
- Length
- 80 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DDEF1_SH3; 19-mer from adenomatous polyposis COLI protein
- UniProt
- Q9ULH1, P25054
Structure
solution nmr · 2 distinct chains · 4% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DDEF1_SH3 | protein | 61 | 5% helix, 48% strand | Q9ULH1 |
| B | 19-mer from adenomatous polyposis COLI protein | protein | 19 | 0% helix, 0% strand | P25054 |
Interfaces
1 interface between chains.
- A–B · 751 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 2RQU · Solution structure of the complex between the DDEF1 SH3 domain and the APC SAMP1 motif · the same entry in another collection · chain A against A, TM-score 1.00
- Q9ULH1 · AlphaFold monomer V2.0 prediction for arf-gap with SH3 domain, ank repeat and pH… · a predicted model of the same protein · chain A against A, TM-score 0.90
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 Q9ULH1
- Every structure of UniProt P25054
- Elsewhere: RCSB PDB 2RQU · PDBe 2RQU · UniProt Q9ULH1 · UniProt P25054
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