PDBe 5cb1

X-ray diffraction
3.3Å resolution

Apo enzyme of human Polymerase lambda

Released:
Source organism: Homo sapiens
Primary publication:
Structural Mechanism for the Fidelity Modulation of DNA Polymerase λ.
J. Am. Chem. Soc. (2016)
PMID: 26836966

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA polymerase lambda Chains: A, B
Molecule details ›
Chains: A, B
Length: 326 amino acids
Theoretical weight: 36.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UGP5 (Residues: 250-575; Coverage: 57%)
Gene name: POLL
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13C1
Spacegroup: I4122
Unit cell:
a: 205.285Å b: 205.285Å c: 111.395Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.23 0.264
Expression system: Escherichia coli