1a5t

CRYSTAL STRUCTURE OF THE DELTA PRIME SUBUNIT OF THE CLAMP-LOADER COMPLEX OF ESCHERICHIA COLI DNA POLYMERASE III

Method: X-RAY DIFFRACTION Dmax: 78.8 Å Quality: GOOD

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

DELTA PRIME

Escherichia coli K12

UniProt P28631

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–334 Not recorded ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.8;277 K;THE PROTEIN WAS CRYSTALLIZED FROM 20-27% PEG 400, 100 MM HEPES, PH6.8, 100 MM MGCL2, 1-3% GLYCEROL, 10MM MGSO4, AT 4C, temperature 277K Resolution 2.20 Å R-free 0.265

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.

34 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HOLB_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–334; UniProt 1–334

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 1a5t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a5t
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1a5t
Deposition date deposition_date1998-02-18
Structure title titleCRYSTAL STRUCTURE OF THE DELTA PRIME SUBUNIT OF THE CLAMP-LOADER COMPLEX OF ESCHERICHIA COLI DNA POLYMERASE III
Keywords keywordsZINC FINGER, DNA REPLICATION; ZINC FINGER
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.24
Radius of gyration Rg (electron density) rg_electron23.27
Forward intensity I(0) i021658400.00
Molecular weight molecular_weight35731.0 kDa
Excluded volume excluded_volume44850 ų
Envelope volume envelope_volume55334 ų
Hydration-shell volume shell_volume20665 ų
Envelope diameter envelope_diameter79.6
Shell Rg shell_rg29.37
Envelope Rg envelope_rg23.04
Shape Rg shape_rg23.26
Total Rg total_rg24.09
Total atoms total_atoms3063
Residues n_residues324
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 dmax78.8
Rg (real space) rg_real24.31
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real2.1660e+07
I(0) uncertainty (real space) i0_real_error3.1500e+05
Rg (reciprocal space) rg_reciprocal24.29
I(0) (reciprocal space) i0_reciprocal21660000.0000
Solution quality estimate total_estimate0.8945
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.6
Skewness Skewness skewness0.373
Kurtosis Kurtosis kurtosis-0.447
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3790000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.908; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.932; Smooth: 0.967

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1a5ta1
Class classa — All alpha proteins
Fold Fold folda.80 — post-AAA+ oligomerization domain-like
Superfamily Superfamily superfamilya.80.1 — post-AAA+ oligomerization domain-like
Family Family familya.80.1.1 — DNA polymerase III clamp loader subunits, C-terminal domain
Domain ID domain_idd1a5ta2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.20 — Extended AAA-ATPase domain

CATH v4.4 (3 domains)

Domain ID domain_id1a5tA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id1a5tA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily10 — Ubiquitin-associated (UBA) domain
Domain ID domain_id1a5tA03
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology272 — Zinc Finger, Delta Prime; domain 3
Homologous superfamily homologous superfamily10

8. Citations (2)

9. Files and Curves (10)