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› 6dqt

X-ray diffraction
1.95Å resolution

Crystal structure of Haemophilus influenzae OppA complex with LGG

Released:
DOI: 10.2210/pdb6dqt/pdb
Model geometry
Fit model/data
PDB entry 6dqt coloured by chain, front view.
PDB entry 6dqt coloured by chain, side view.
PDB entry 6dqt coloured by chain, top view.
Source organism: Haemophilus influenzae 86-028NP
Primary publication:
Oligopeptide-binding protein from nontypeable Haemophilus influenzae has ligand-specific sites to accommodate peptides and heme in the binding pocket.
Tanaka KJ, Pinkett HW
J Biol Chem 294 1070-1082 (2019)
PMID: 30455346

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-166620 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Solute-binding protein family 5 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 530 amino acids
Theoretical weight: 59.99 KDa
Source organism: Haemophilus influenzae 86-028NP
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q4QLH0 (Residues: 21-541; Coverage: 100%)
Gene names: NTHI1292, oppA
Sequence domains: Bacterial extracellular solute-binding proteins, family 5 Middle
Structure domains:
LEU-GLY-GLY Chain: B
Molecule details ›
Chain: B
Length: 3 amino acids
Theoretical weight: 245 Da
Source organism: Haemophilus influenzae 86-028NP
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand ACT 3 x ACT
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P212121
Unit cell:
a: 49.522Å b: 90.953Å c: 108.86Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.166 0.205
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

8 citation in other articles

Moonlighting of Haemophilus influenzae heme acquisition systems contributes to the host airway-pathogen interplay in a coordinated manner.
Rodríguez-Arce et al. (2019)
7 more

1 mention without citation

Oligopeptide-binding protein from nontypeable Haemophilus influenzae has ligand-specific sites to accommodate peptides and heme in the binding pocket.
Tanaka et al. (2019)