Research workbench
Molecular and structural characterization of the SH3 domain of ahi-1 in regulation of cellular resistance of BCR-abl+ chronic myeloid leukemia cells to tyrosine kinase inhibitors
Analyse Molecular and structural characterization of the SH3 domain of ahi-1 in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ESR
- Type
- protein
- Length
- 129 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Jouberin
- UniProt
- Q8N157
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Jouberin | protein | 65 | 14% helix, 46% strand | Q8N157 |
| B | Jouberin | protein | 64 | 13% helix, 47% strand | Q8N157 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 359 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 4ESR · Molecular and Structural Characterization of the SH3 Domain of AHI-1 in Regulation of… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8N157 · AlphaFold monomer V2.0 prediction for jouberin (Q8N157) · a predicted model of the same protein · chain B against A, TM-score 0.92
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 Q8N157
- Elsewhere: RCSB PDB 4ESR · PDBe 4ESR · UniProt Q8N157
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