5ot2

X-ray diffraction
3.2Å resolution

RNA polymerase II elongation complex in the presence of 3d-Napht-A

Released:
Model geometry
Fit model/data
Primary publication:
Mechanism of RNA polymerase II stalling by DNA alkylation.
OpenAccess logo Proc Natl Acad Sci U S A 114 12172-12177 (2017)
PMID: 29087308

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero pentadecamer (preferred)
PDBe Complex ID:
PDB-CPX-119116 (preferred)
Entry contents:
12 distinct polypeptide molecules
2 distinct DNA molecules
1 distinct RNA molecule
Macromolecules (15 distinct):
DNA-directed RNA polymerase II subunit RPB1 Chain: A
DNA-directed RNA polymerase II subunit RPB2 Chain: B
DNA-directed RNA polymerase II subunit RPB3 Chain: C
DNA-directed RNA polymerase II subunit RPB4 Chain: D
DNA-directed RNA polymerases I, II, and III subunit RPABC1 Chain: E
DNA-directed RNA polymerases I, II, and III subunit RPABC2 Chain: F
DNA-directed RNA polymerase II subunit RPB7 Chain: G
DNA-directed RNA polymerases I, II, and III subunit RPABC3 Chain: H
DNA-directed RNA polymerase II subunit RPB9 Chain: I
DNA-directed RNA polymerases I, II, and III subunit RPABC5 Chain: J
DNA-directed RNA polymerase II subunit RPB11 Chain: K
DNA-directed RNA polymerases I, II, and III subunit RPABC4 Chain: L
DNA template strand Chain: T
DNA non-template strand Chain: N
RNA product strand Chain: P

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Spacegroup: C2221
Unit cell:
a: 221.35Å b: 394.93Å c: 283.71Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.178 0.222