Research workbench
NMR structure of the C-terminal coiled-coil domain of CIN85
Analyse NMR structure of the C-terminal coiled-coil domain of CIN85 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2N64
- Type
- protein
- Length
- 225 residues
- Chains
- 3
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SH3 domain-containing kinase-binding protein 1
- UniProt
- Q96B97
Structure
solution nmr · 1 distinct chain · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | SH3 domain-containing kinase-binding protein 1 | protein | 75 | 79% helix, 0% strand | Q96B97 |
Interfaces
3 interfaces between chains.
- B–C · 1991 Ų buried · 24 hydrogen bonds · protein-protein
- A–B · 1990 Ų buried · 24 hydrogen bonds · protein-protein
- A–C · 1984 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 2N64 · NMR Structure of the C-terminal Coiled-Coil Domain of CIN85 · the same entry in another collection · chain A against A, TM-score 1.00
- Q96B97 · AlphaFold monomer V2.0 prediction for SH3 domain-containing kinase- binding protein 1… · a predicted model of the same protein · chain A against A, TM-score 0.69
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 Q96B97
- Elsewhere: RCSB PDB 2N64 · PDBe 2N64 · UniProt Q96B97
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