5i7m

Crystal structure of Y345F mutant of human primase p58 iron-sulfur cluster domain

Method: X-RAY DIFFRACTION Dmax: 72.9 Å Quality: GOOD

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

DNA primase large subunit

Homo sapiens

UniProt P49643

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 272–457 Chain B; UniProt 272–457 Fragment:iron-sulfur cluster domain (UNP residues 272-457) Mutation:Y345F SF4 IRON/SULFUR CLUSTER × 2 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;75 mg/mL p58C Y345F in 20 mM MES, pH 6.5, 50 mM sodium chloride, reservoir solution: 100 mM Tris, pH 8.5, 150 mM lithium sulfate, 18% PEG3350 Resolution 1.93 Å R-free 0.250

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.

21 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRI2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–188; UniProt 272–457 Author chain B; PDBConstruct 3–188; UniProt 272–457

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 5i7m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5i7m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5i7m
Deposition date deposition_date2016-02-17
Structure title titleCrystal structure of Y345F mutant of human primase p58 iron-sulfur cluster domain
Keywords keywordsDNA replication, primase, [4Fe-4S], p58C, REPLICATION; REPLICATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.49
Radius of gyration Rg (electron density) rg_electron21.79
Forward intensity I(0) i026484200.00
Molecular weight molecular_weight38012.0 kDa
Excluded volume excluded_volume46881 ų
Envelope volume envelope_volume56972 ų
Hydration-shell volume shell_volume22114 ų
Envelope diameter envelope_diameter77.5
Shell Rg shell_rg28.14
Envelope Rg envelope_rg22.33
Shape Rg shape_rg21.86
Total Rg total_rg22.38
Total atoms total_atoms2644
Residues n_residues329
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 dmax72.9
Rg (real space) rg_real22.49
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real2.6480e+07
I(0) uncertainty (real space) i0_real_error3.4650e+05
Rg (reciprocal space) rg_reciprocal22.49
I(0) (reciprocal space) i0_reciprocal26480000.0000
Solution quality estimate total_estimate0.8169
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.3
Skewness Skewness skewness0.329
Kurtosis Kurtosis kurtosis-0.440
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8855000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.876; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)