› 3gmx

X-ray diffraction
1.05Å resolution

Crystal Structure of Beta-Lactamse Inhibitory Protein-Like Protein (BLP) at 1.05 Angstrom Resolution

Released:
DOI: 10.2210/pdb3gmx/pdb
PDB entry 3gmx coloured by chain, front view.
PDB entry 3gmx coloured by chain, side view.
PDB entry 3gmx 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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110203 (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: 17.55 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

1 bound ligand:
Ligand ACT 4 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P21
Unit cell:
a: 35.771Å b: 99.925Å c: 41.643Å
α: 90° β: 101.26° γ: 90°
R-values:
R R work R free
0.126 0.125 0.154
Expression system: Escherichia coli

Quick links

Citations

5 review citations

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

2 mentions without citation

Structural basis of outer membrane protein biogenesis in bacteria.
Albrecht et al. (2011)
1 more