› 5fhh

X-ray diffraction
3.6Å resolution

Structure of human Pif1 helicase domain residues 200-641

Released:
DOI: 10.2210/pdb5fhh/pdb
PDB entry 5fhh coloured by chain, front view.
PDB entry 5fhh coloured by chain, side view.
PDB entry 5fhh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and Functional Insights into the Unwinding Mechanism of Bacteroides sp Pif1.
Zhou X, Ren W, Bharath SR, Tang X, He Y, Chen C, Liu Z, Li D, Song H
Cell Rep 14 2030-9 (2016)
PMID: 26904952

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190630 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent DNA helicase PIF1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 442 amino acids
Theoretical weight: 48.01 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H611 (Residues: 200-641; Coverage: 69%)
Gene names: C15orf20, PIF1
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand ADP 2 x ADP
Ligand ALF 2 x ALF
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P3221
Unit cell:
a: 204.75Å b: 204.75Å c: 77.791Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.312 0.31 0.355
Expression system: Escherichia coli

Quick links

Citations

7 review citations

The functions of the multi-tasking Pfh1Pif1 helicase.
Sabouri N. (2017)
6 more

5 mentions without citation

Structure and function of Pif1 helicase.
Byrd et al. (2017)
4 more