4bpw

Crystal structure of human primase bound to UTP

Method: X-RAY DIFFRACTION Dmax: 138.5 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:PRIS Mutation:YES ZN ZINC ION × 1 MG MAGNESIUM ION × 2 UTP URIDINE 5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:100MM TRIS-HCL/BICINE PH 8.5, 20% GLYCEROL, 10% PEG4000 AND 20MM EACH OF AN ALCOHOL MIX COMPRISING 1,6-HEXANEDIOL, 1-BUTANOL, 1,2-PROPANEDIOL, 2-PROPANOL, 1,4-BUTANEDIOL AND 1,3-PROPANEDIOL. Resolution 3.00 Å R-free 0.253
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 1–420 Fragment:PRIS Mutation:YES ZN ZINC ION × 1 MG MAGNESIUM ION × 2 UTP URIDINE 5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:100MM TRIS-HCL/BICINE PH 8.5, 20% GLYCEROL, 10% PEG4000 AND 20MM EACH OF AN ALCOHOL MIX COMPRISING 1,6-HEXANEDIOL, 1-BUTANOL, 1,2-PROPANEDIOL, 2-PROPANOL, 1,4-BUTANEDIOL AND 1,3-PROPANEDIOL. Resolution 3.00 Å R-free 0.253

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 31 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 4–423; UniProt 1–420 Author chain C; PDBConstruct 4–423; UniProt 1–420

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
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–253 Fragment:PRIL, RESIDUES 1-253 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:100MM TRIS-HCL/BICINE PH 8.5, 20% GLYCEROL, 10% PEG4000 AND 20MM EACH OF AN ALCOHOL MIX COMPRISING 1,6-HEXANEDIOL, 1-BUTANOL, 1,2-PROPANEDIOL, 2-PROPANOL, 1,4-BUTANEDIOL AND 1,3-PROPANEDIOL. Resolution 3.00 Å R-free 0.253
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 1–253 Fragment:PRIL, RESIDUES 1-253 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:100MM TRIS-HCL/BICINE PH 8.5, 20% GLYCEROL, 10% PEG4000 AND 20MM EACH OF AN ALCOHOL MIX COMPRISING 1,6-HEXANEDIOL, 1-BUTANOL, 1,2-PROPANEDIOL, 2-PROPANOL, 1,4-BUTANEDIOL AND 1,3-PROPANEDIOL. Resolution 3.00 Å R-free 0.253

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 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRI2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–253; UniProt 1–253 Author chain D; PDBConstruct 1–253; UniProt 1–253

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 4bpw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4bpw
Deposition date deposition_date2013-05-28
Structure title titleCrystal structure of human primase bound to UTP
Keywords keywordsTRANSFERASE, DNA-DEPENDENT RNA POLYMERASE, DNA REPLICATION; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier41.93
Radius of gyration Rg (electron density) rg_electron41.58
Forward intensity I(0) i0280491000.00
Molecular weight molecular_weight139640.0 kDa
Excluded volume excluded_volume176120 ų
Envelope volume envelope_volume253030 ų
Hydration-shell volume shell_volume52128 ų
Envelope diameter envelope_diameter140.3
Shell Rg shell_rg45.73
Envelope Rg envelope_rg39.99
Shape Rg shape_rg41.57
Total Rg total_rg41.88
Total atoms total_atoms19712
Residues n_residues1176
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 dmax138.5
Rg (real space) rg_real41.99
Rg uncertainty (real space) rg_real_error1.15
I(0) (real space) i0_real2.8050e+08
I(0) uncertainty (real space) i0_real_error5.3630e+06
Rg (reciprocal space) rg_reciprocal41.93
I(0) (reciprocal space) i0_reciprocal280500000.0000
Solution quality estimate total_estimate0.8900
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.4
Skewness Skewness skewness0.285
Kurtosis Kurtosis kurtosis-0.651
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21500000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.892; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.913

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id4bpwA00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology920 — DNA primase, PRIM domain
Homologous superfamily homologous superfamily10 — DNA primase, PRIM domain
Domain ID domain_id4bpwB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology930 — Transcription Elongation Factor S-II; Chain A
Homologous superfamily homologous superfamily80
Domain ID domain_id4bpwC00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology920 — DNA primase, PRIM domain
Homologous superfamily homologous superfamily10 — DNA primase, PRIM domain
Domain ID domain_id4bpwD00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology930 — Transcription Elongation Factor S-II; Chain A
Homologous superfamily homologous superfamily80

8. Citations (1)

9. Files and Curves (10)