4lil

Crystal structure of the catalytic subunit of human primase bound to UTP and Mn

Method: X-RAY DIFFRACTION Dmax: 81.2 Å Quality: GOOD

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

DNA primase small subunit

Homo sapiens

UniProt P49642

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 1–408 Fragment:Catalytic subunit p48, UNP residues 1-390 (delta 360-379) ZN ZINC ION × 1 MN MANGANESE (II) ION × 2 UTP URIDINE 5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;294 K;0.2M K/Na Tartrate and 20% PEG 3350, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 294K Resolution 2.60 Å R-free 0.248

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.

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

View Construct and Data Evidence
UniProt name PRI1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–392; UniProt 1–408

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 4lil

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4lil
Deposition date deposition_date2013-07-02
Structure title titleCrystal structure of the catalytic subunit of human primase bound to UTP and Mn
Keywords keywordsPrim fold, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.43
Radius of gyration Rg (electron density) rg_electron23.60
Forward intensity I(0) i032660100.00
Molecular weight molecular_weight44498.0 kDa
Excluded volume excluded_volume55855 ų
Envelope volume envelope_volume66179 ų
Hydration-shell volume shell_volume24159 ų
Envelope diameter envelope_diameter84.0
Shell Rg shell_rg29.99
Envelope Rg envelope_rg24.09
Shape Rg shape_rg23.63
Total Rg total_rg24.26
Total atoms total_atoms3129
Residues n_residues370
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 dmax81.2
Rg (real space) rg_real24.54
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real3.2660e+07
I(0) uncertainty (real space) i0_real_error4.9480e+05
Rg (reciprocal space) rg_reciprocal24.52
I(0) (reciprocal space) i0_reciprocal32660000.0000
Solution quality estimate total_estimate0.8725
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.8
Skewness Skewness skewness0.480
Kurtosis Kurtosis kurtosis-0.272
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5945000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.813; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.924; Smooth: 0.975

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id4lilA00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology920 — DNA primase, PRIM domain
Homologous superfamily homologous superfamily10 — DNA primase, PRIM domain

8. Citations (1)

9. Files and Curves (10)