4k3q

E. coli sliding clamp in complex with AcQLDAF

Method: X-RAY DIFFRACTION Dmax: 97.5 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

DNA polymerase III subunit beta

Escherichia coli

UniProt P0A988

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–366 Chain B; UniProt 1–366 Not recorded (ACE)QLDAF × 1 PEG DI(HYDROXYETHYL)ETHER × 6 CA CALCIUM ION × 7 PGE TRIETHYLENE GLYCOL × 3 PG4 TETRAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;285 K;100mM MES, 100-150mM CaCl2, 25-30%(v/v) PEG400, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 285K Resolution 1.85 Å R-free 0.242

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

53 other PDB entries and 60 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPO3B_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–366; UniProt 1–366 Author chain B; PDBConstruct 1–366; UniProt 1–366

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 4k3q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4k3q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4k3q
Deposition date deposition_date2013-04-11
Structure title titleE. coli sliding clamp in complex with AcQLDAF
Keywords keywordsE. coli sliding clamp, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier33.27
Radius of gyration Rg (electron density) rg_electron32.10
Forward intensity I(0) i0105596000.00
Molecular weight molecular_weight81132.0 kDa
Excluded volume excluded_volume101510 ų
Envelope volume envelope_volume140670 ų
Hydration-shell volume shell_volume35719 ų
Envelope diameter envelope_diameter95.4
Shell Rg shell_rg40.48
Envelope Rg envelope_rg30.56
Shape Rg shape_rg32.11
Total Rg total_rg32.79
Total atoms total_atoms5670
Residues n_residues721
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax97.5
Rg (real space) rg_real33.05
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real1.0560e+08
I(0) uncertainty (real space) i0_real_error1.7760e+06
Rg (reciprocal space) rg_reciprocal33.15
I(0) (reciprocal space) i0_reciprocal105600000.0000
Solution quality estimate total_estimate0.8988
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary50.8
Skewness Skewness skewness-0.050
Kurtosis Kurtosis kurtosis-0.868
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha84080000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.913; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.943

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id4k3qA01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology150 — DNA Polymerase III; Chain A, domain 2
Homologous superfamily homologous superfamily10 — DNA Polymerase III, subunit A, domain 2
Domain ID domain_id4k3qA02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology150 — DNA Polymerase III; Chain A, domain 2
Homologous superfamily homologous superfamily10 — DNA Polymerase III, subunit A, domain 2
Domain ID domain_id4k3qA03
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology150 — DNA Polymerase III; Chain A, domain 2
Homologous superfamily homologous superfamily10 — DNA Polymerase III, subunit A, domain 2
Domain ID domain_id4k3qB01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology150 — DNA Polymerase III; Chain A, domain 2
Homologous superfamily homologous superfamily10 — DNA Polymerase III, subunit A, domain 2
Domain ID domain_id4k3qB02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology150 — DNA Polymerase III; Chain A, domain 2
Homologous superfamily homologous superfamily10 — DNA Polymerase III, subunit A, domain 2
Domain ID domain_id4k3qB03
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology150 — DNA Polymerase III; Chain A, domain 2
Homologous superfamily homologous superfamily10 — DNA Polymerase III, subunit A, domain 2

8. Citations (1)

9. Files and Curves (10)