- PDB-3bgw: The Structure Of A DnaB-Like Replicative Helicase And Its Interac... -
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ID or keywords:
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Basic information
Entry
Database: PDB / ID: 3bgw
Title
The Structure Of A DnaB-Like Replicative Helicase And Its Interactions With Primase
Components
DNAB-Like Replicative Helicase
Keywords
REPLICATION / ATPase
Function / homology
Function and homology information
double-stranded DNA helicase activity / DNA unwinding involved in DNA replication / DNA helicase / hydrolase activity / DNA binding / ATP binding / identical protein binding / cytosol Similarity search - Function
DNAb Helicase; Chain A / DNAb Helicase; Chain A / DNA helicase, DnaB type / DNA helicase, DnaB-like, N-terminal / DnaB-like helicase N terminal domain / DNA helicase, DnaB-like, N-terminal domain superfamily / DNA helicase DnaB, N-terminal/DNA primase DnaG, C-terminal / DnaB-like helicase C terminal domain / DNA helicase, DnaB-like, C-terminal / Superfamily 4 helicase domain profile. ...DNAb Helicase; Chain A / DNAb Helicase; Chain A / DNA helicase, DnaB type / DNA helicase, DnaB-like, N-terminal / DnaB-like helicase N terminal domain / DNA helicase, DnaB-like, N-terminal domain superfamily / DNA helicase DnaB, N-terminal/DNA primase DnaG, C-terminal / DnaB-like helicase C terminal domain / DNA helicase, DnaB-like, C-terminal / Superfamily 4 helicase domain profile. / P-loop containing nucleotide triphosphate hydrolases / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta Similarity search - Domain/homology
Resolution: 3.9→4.04 Å / Redundancy: 6.4 % / Rmerge(I) obs: 0.0508 / Mean I/σ(I) obs: 2.5 / Num. unique all: 3242 / Rsym value: 0.082 / % possible all: 92.1
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Processing
Software
Name
Version
Classification
REFMAC
5.2.0019
refinement
HKL-2000
datacollection
HKL-2000
datareduction
HKL-2000
datascaling
SOLVE
phasing
Refinement
Method to determine structure: SAD / Resolution: 3.91→38.81 Å / Cor.coef. Fo:Fc: 0.825 / Cor.coef. Fo:Fc free: 0.811 / SU B: 159.178 / SU ML: 0.983 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 1.077 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: Hydrogens have been added in the riding positions.The bad geometry on ASN174 in chains A and F is due to low resolution. The structure is the best authors can do at this resolution with the ...Details: Hydrogens have been added in the riding positions.The bad geometry on ASN174 in chains A and F is due to low resolution. The structure is the best authors can do at this resolution with the currently available crystallography program.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.34889
1750
5 %
RANDOM
Rwork
0.33801
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obs
0.33858
33329
97.45 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK