› 4pvk

X-ray diffraction
1.3Å resolution

Phl p 4 I153V N158H variant, a glucose oxidase

Released:
DOI: 10.2210/pdb4pvk/pdb
PDB entry 4pvk coloured by chain, front view.
PDB entry 4pvk coloured by chain, side view.
PDB entry 4pvk coloured by chain, top view.
Source organism: Phleum pratense
Primary publication:
Rationally engineered flavin-dependent oxidase reveals steric control of dioxygen reduction.
Zafred D, Steiner B, Teufelberger AR, Hromic A, Karplus PA, Schofield CJ, Wallner S, Macheroux P
FEBS J 282 3060-74 (2015)
PMID: 25619330

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109786 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FAD-binding PCMH-type domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 500 amino acids
Theoretical weight: 55.74 KDa
Source organism: Phleum pratense
Expression system: Komagataella pastoris
UniProt:
  • Canonical: B2ZWE9 (Residues: 1-500; Coverage: 100%)
Gene name: phlp4
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand FAD 1 x FAD
Ligand NA 2 x NA
Ligand CL 1 x CL
Ligand MLI 2 x MLI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P6122
Unit cell:
a: 117.37Å b: 117.37Å c: 201Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.142 0.141 0.16
Expression system: Komagataella pastoris

Quick links

Citations

3 review citations

Sweating the assets of flavin cofactors: new insight of chemical versatility from knowledge of structure and mechanism.
Leys et al. (2016)
2 more

3 mentions without citation

Self-association of a highly charged arginine-rich cell-penetrating peptide.
Tesei et al. (2017)
2 more