MolNFT v1 · #50665 · protein
A crucial role for high intrinsic specificity in the function of yeast SH3 domains
2RPN · Actin-binding protein: “A crucial role for high intrinsic specificity in the function of yeast SH3 domains”. Solution nmr. MolNFT v1 #50665 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2RPN
- Type
- protein
- Length
- 77 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actin-binding protein; Actin-regulating kinase 1
- UniProt
- P15891, P53974
Structure
solution nmr · 2 distinct chains · 4% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Actin-binding protein | protein | 59 | 5% helix, 42% strand | P15891 |
| B | Actin-regulating kinase 1 | protein | 18 | 0% helix, 0% strand | P53974 |
Interfaces
1 interface between chains.
- A–B · 652 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 2RPN · A crucial role for high intrinsic specificity in the function of yeast SH3 domains · the same entry in another collection · chain A against A, TM-score 1.00
- P15891 · AlphaFold monomer V2.0 prediction for actin-binding protein (P15891) · a predicted model of the same protein · chain A against A, TM-score 0.86
- P53974 · AlphaFold monomer V2.0 prediction for actin-regulating kinase 1 (P53974) · a predicted model of the same protein · chain B against A, TM-score 0.23
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 P15891
- Every structure of UniProt P53974
- Elsewhere: RCSB PDB 2RPN · PDBe 2RPN · UniProt P15891 · UniProt P53974
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