› 6ipy

X-ray diffraction
1.34Å resolution

His-tagged Fyn SH3 domain R96I mutant

Released:
DOI: 10.2210/pdb6ipy/pdb
PDB entry 6ipy coloured by chain, front view.
PDB entry 6ipy coloured by chain, side view.
PDB entry 6ipy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Synergy and allostery in ligand binding by HIV-1 Nef.
Aldehaiman A, Momin AA, Restouin A, Wang L, Shi X, Aljedani S, Opi S, Lugari A, Shahul Hameed UF, Ponchon L, Morelli X, Huang M, Dumas C, Collette Y, Arold ST
Biochem J 478 1525-1545 (2021)
PMID: 33787846

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138961 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase Fyn Chain: A
Molecule details ›
Chain: A
Length: 81 amino acids
Theoretical weight: 9.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P06241 (Residues: 82-144; Coverage: 12%)
Gene name: FYN
Sequence domains: SH3 domain
Structure domains: SH3 Domains

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 2
Spacegroup: P41
Unit cell:
a: 41.52Å b: 41.52Å c: 32.64Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.181 0.201
Expression system: Escherichia coli BL21

Quick links

Citations

2 citation in other articles

Evolutionary plasticity of SH3 domain binding by Nef proteins of the HIV-1/SIVcpz lentiviral lineage.
Zhao et al. (2021)
1 more

1 mention without citation

Synergy and allostery in ligand binding by HIV-1 Nef.
Aldehaiman et al. (2021)