› 5iqw

X-ray diffraction
1.95Å resolution

1.95A resolution structure of Apo HasAp (R33A) from Pseudomonas aeruginosa

Released:
DOI: 10.2210/pdb5iqw/pdb
PDB entry 5iqw coloured by chain, front view.
PDB entry 5iqw coloured by chain, side view.
PDB entry 5iqw coloured by chain, top view.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
Replacing Arginine 33 for Alanine in the Hemophore HasA from Pseudomonas aeruginosa Causes Closure of the H32 Loop in the Apo-Protein.
Kumar R, Qi Y, Matsumura H, Lovell S, Yao H, Battaile KP, Im W, Moënne-Loccoz P, Rivera M
Biochemistry 55 2622-31 (2016)
PMID: 27074415

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-124397 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heme acquisition protein HasAp Chain: A
Molecule details ›
Chain: A
Length: 184 amino acids
Theoretical weight: 18.82 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli
UniProt:
  • Canonical: G3XD33 (Residues: 1-184; Coverage: 90%)
Gene names: PA3407, hasAp
Sequence domains: Heme-binding protein A (HasA)
Structure domains: Haem-binding HasA

Ligands and Environments

2 bound ligands:
Ligand ACT 1 x ACT
Ligand CD 3 x CD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P41212
Unit cell:
a: 92.781Å b: 92.781Å c: 95.714Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.185 0.212
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Extracellular Heme Uptake and the Challenge of Bacterial Cell Membranes.
Huang et al. (2017)
1 more

1 mention without citation

Replacing Arginine 33 for Alanine in the Hemophore HasA from Pseudomonas aeruginosa Causes Closure of the H32 Loop in the Apo-Protein.
Kumar et al. (2016)