› 3gmy

X-ray diffraction
1.7Å resolution

Crystal Structure of Beta-Lactamse Inhibitory Protein-Like Protein (BLP), Selenomethionine Derivative

Released:
DOI: 10.2210/pdb3gmy/pdb
PDB entry 3gmy coloured by chain, front view.
PDB entry 3gmy coloured by chain, side view.
PDB entry 3gmy coloured by chain, top view.
Source organism: Streptomyces clavuligerus
Primary publication:
Insights into positive and negative requirements for protein-protein interactions by crystallographic analysis of the beta-lactamase inhibitory proteins BLIP, BLIP-I, and BLP.
Gretes M, Lim DC, de Castro L, Jensen SE, Kang SG, Lee KJ, Strynadka NC
J Mol Biol 389 289-305 (2009)
PMID: 19332077

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-110202 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-Lactamase Inhibitory Protein-Like Protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 154 amino acids
Theoretical weight: 17.74 KDa
Source organism: Streptomyces clavuligerus
Expression system: Escherichia coli
UniProt:
  • Canonical: B5GLC0 (Residues: 29-182; Coverage: 100%)
Gene names: SCLAV_4202, blp
Sequence domains: Beta-lactamase inhibitor (BLIP)
Structure domains: BLIP domain

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P212121
Unit cell:
a: 101.167Å b: 67.195Å c: 41.208Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.2 0.273
Expression system: Escherichia coli

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Citations

5 review citations

Protein binding specificity versus promiscuity.
Schreiber et al. (2011)
4 more