› 1z3k

Solution NMR

Structural Insight into the Binding Diversity between the Tyr-Phosphorylated Human EphrinBs and Nck2 SH2 Domain

Released:
DOI: 10.2210/pdb1z3k/pdb
PDB entry 1z3k coloured by chain, ensemble of 10 models, front view.
PDB entry 1z3k coloured by chain, ensemble of 10 models, side view.
PDB entry 1z3k coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural insight into the binding diversity between the Tyr-phosphorylated human ephrinBs and Nck2 SH2 domain.
Ran X, Song J
J Biol Chem 280 19205-12 (2005)
PMID: 15764601

Function and Biology Details

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-129043 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytoplasmic protein NCK2 Chain: A
Molecule details ›
Chain: A
Length: 98 amino acids
Theoretical weight: 11.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O43639 (Residues: 283-380; Coverage: 26%)
Gene names: GRB4, NCK2
Sequence domains: SH2 domain
Structure domains: SH2 domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry, simulated annealing
Expression system: Escherichia coli

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Citations

2 review citations

Bidirectional ephrin/Eph signaling in synaptic functions.
Aoto et al. (2007)
1 more

1 mention without citation

Nonnatural protein-protein interaction-pair design by key residues grafting.
Liu et al. (2007)