4mhq

Crystal structure of human primase catalytic subunit

Method: X-RAY DIFFRACTION Dmax: 81.6 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 1–420 Fragment:Full length ZN ZINC ION × 1 CIT CITRIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;294 K;0.1M Na-acetate, 0.2M Tri-Na-citrate, 20% PEG3350, 0.1M Na-acetate , pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 2.20 Å R-free 0.233

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 6–425; UniProt 1–420

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 4mhq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4mhq
Deposition date deposition_date2013-08-30
Structure title titleCrystal structure of human primase catalytic subunit
Keywords keywordsZinc finger, Primase, NTP binding, Nucleus, REPLICATION; REPLICATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.12
Radius of gyration Rg (electron density) rg_electron24.18
Forward intensity I(0) i036793200.00
Molecular weight molecular_weight47762.0 kDa
Excluded volume excluded_volume60173 ų
Envelope volume envelope_volume73347 ų
Hydration-shell volume shell_volume25840 ų
Envelope diameter envelope_diameter85.3
Shell Rg shell_rg30.84
Envelope Rg envelope_rg24.83
Shape Rg shape_rg24.17
Total Rg total_rg24.99
Total atoms total_atoms3367
Residues n_residues400
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 dmax81.6
Rg (real space) rg_real25.17
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real3.6790e+07
I(0) uncertainty (real space) i0_real_error4.7610e+05
Rg (reciprocal space) rg_reciprocal25.16
I(0) (reciprocal space) i0_reciprocal36790000.0000
Solution quality estimate total_estimate0.8877
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.2
Skewness Skewness skewness0.430
Kurtosis Kurtosis kurtosis-0.330
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6710000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.865; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.957; Smooth: 0.984

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id4mhqA00
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)