› 1sem

X-ray diffraction
2Å resolution

STRUCTURAL DETERMINANTS OF PEPTIDE-BINDING ORIENTATION AND OF SEQUENCE SPECIFICITY IN SH3 DOMAINS

Released:
DOI: 10.2210/pdb1sem/pdb
PDB entry 1sem coloured by chain, front view.
PDB entry 1sem coloured by chain, side view.
PDB entry 1sem coloured by chain, top view.
Source organisms:
Primary publication:
Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains.
Lim WA, Richards FM, Fox RO
Nature 372 375-9 (1994)
PMID: 7802869

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151425 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Sex muscle abnormal protein 5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 58 amino acids
Theoretical weight: 6.8 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli
UniProt:
  • Canonical: P29355 (Residues: 155-212; Coverage: 25%)
Gene names: C14F5.5, sem-5
Sequence domains: SH3 domain
Structure domains: SH3 Domains
10-RESIDUE PROLINE-RICH PEPTIDE FROM MSOS (ACE-PRO-PRO-PRO-VAL-PRO-PRO-ARG-ARG-ARG) Chains: C, D
Molecule details ›
Chains: C, D
Length: 10 amino acids
Theoretical weight: 1.1 KDa
Source organism: Mus musculus

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 26.912Å b: 68.41Å c: 35.029Å
α: 90° β: 94.71° γ: 90°
R-values:
R R work R free
0.189 0.189 not available
Expression system: Escherichia coli

Quick links

Citations

59 review citations

Protein modules and signalling networks.
Pawson T. (1995)
58 more

26 mentions without citation

Site-directed spectroscopic probes of actomyosin structural dynamics.
Thomas et al. (2009)
25 more