4fvm

Crystal structure of yeast DNA polymerase alpha

Method: X-RAY DIFFRACTION Dmax: 105.2 Å Quality: GOOD

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

DNA polymerase alpha catalytic subunit A

Saccharomyces cerevisiae

UniProt P13382

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 349–1258 Fragment:Polymerase domain, UNP residues 349-1258 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9.4;291 K;0.1M Bicine, 6% PEG8000, pH 9.4, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.30 Å R-free 0.236

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.

9 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPOA_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–910; UniProt 349–1258

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 4fvm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4fvm
Deposition date deposition_date2012-06-29
Structure title titleCrystal structure of yeast DNA polymerase alpha
Keywords keywordsDNA Polymerase, DNA replication, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.37
Radius of gyration Rg (electron density) rg_electron31.66
Forward intensity I(0) i0139783000.00
Molecular weight molecular_weight94540.0 kDa
Excluded volume excluded_volume118780 ų
Envelope volume envelope_volume159240 ų
Hydration-shell volume shell_volume41596 ų
Envelope diameter envelope_diameter109.8
Shell Rg shell_rg39.02
Envelope Rg envelope_rg31.29
Shape Rg shape_rg31.67
Total Rg total_rg32.25
Total atoms total_atoms13359
Residues n_residues829
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 dmax105.2
Rg (real space) rg_real32.28
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real1.3980e+08
I(0) uncertainty (real space) i0_real_error2.2650e+06
Rg (reciprocal space) rg_reciprocal32.32
I(0) (reciprocal space) i0_reciprocal139800000.0000
Solution quality estimate total_estimate0.8932
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.6
Skewness Skewness skewness0.233
Kurtosis Kurtosis kurtosis-0.456
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha28550000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.910; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.879

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id4fvmA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily730
Domain ID domain_id4fvmA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily2820
Domain ID domain_id4fvmA03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily10 — Ribonuclease H-like superfamily/Ribonuclease H
Domain ID domain_id4fvmA04
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology10 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily100
Domain ID domain_id4fvmA05
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1600 — Palm domain of DNA polymerase
Homologous superfamily homologous superfamily10 — B family DNA polymerase, palm domain
Domain ID domain_id4fvmA06
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily690 — B family DNA polymerase, finger domain
Domain ID domain_id4fvmA07
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily310 — B family DNA polymerase, thumb domain, four helix bundle
Domain ID domain_id4fvmA08
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1820 — Ribonuclease H-like motif
Homologous superfamily homologous superfamily20 — B family DNA polymerase, thumb domain, alpha/beta motif

8. Citations (1)

9. Files and Curves (10)