8zp5

Cryo-EM structure of origin recognition complex (Orc5 basic patch mutations) with ARS1 DNA bound

Method: ELECTRON MICROSCOPY Dmax: 156.9 Å Quality: GOOD

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

Origin recognition complex subunit 2

Saccharomyces cerevisiae S288C

UniProt P32833

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–DNA Heteromer Protein × 6 DNA 2 PDB declaration: octameric(8) Consistent with all polymer counts Chain B; UniProt 1–620 Not recorded Origin recognition complex subunit 5 × 1 (P50874) Origin recognition complex subunit 6 × 1 (P38826) DNA (35-MER) × 1 DNA (34-MER) × 1 Origin recognition complex subunit 1 × 1 (P54784) Origin recognition complex subunit 3 × 1 (P54790) Origin recognition complex subunit 4 × 1 (P54791) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.98 Å

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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ORC2_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–620; UniProt 1–620

Origin recognition complex subunit 5

Saccharomyces cerevisiae S288C

UniProt P50874

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–DNA Heteromer Protein × 6 DNA 2 PDB declaration: octameric(8) Consistent with all polymer counts Chain E; UniProt 1–479 Mutation:R360A, R366A, K367A Origin recognition complex subunit 2 × 1 (P32833) Origin recognition complex subunit 6 × 1 (P38826) DNA (35-MER) × 1 DNA (34-MER) × 1 Origin recognition complex subunit 1 × 1 (P54784) Origin recognition complex subunit 3 × 1 (P54790) Origin recognition complex subunit 4 × 1 (P54791) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.98 Å

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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ORC5_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–479; UniProt 1–479

Origin recognition complex subunit 6

Saccharomyces cerevisiae S288C

UniProt P38826

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–DNA Heteromer Protein × 6 DNA 2 PDB declaration: octameric(8) Consistent with all polymer counts Chain F; UniProt 1–435 Not recorded Origin recognition complex subunit 2 × 1 (P32833) Origin recognition complex subunit 5 × 1 (P50874) DNA (35-MER) × 1 DNA (34-MER) × 1 Origin recognition complex subunit 1 × 1 (P54784) Origin recognition complex subunit 3 × 1 (P54790) Origin recognition complex subunit 4 × 1 (P54791) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.98 Å

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.

18 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ORC6_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain F; PDBConstruct 1–435; UniProt 1–435

Origin recognition complex subunit 1

Saccharomyces cerevisiae S288C

UniProt P54784

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–DNA Heteromer Protein × 6 DNA 2 PDB declaration: octameric(8) Consistent with all polymer counts Chain A; UniProt 1–914 Not recorded Origin recognition complex subunit 2 × 1 (P32833) Origin recognition complex subunit 5 × 1 (P50874) Origin recognition complex subunit 6 × 1 (P38826) DNA (35-MER) × 1 DNA (34-MER) × 1 Origin recognition complex subunit 3 × 1 (P54790) Origin recognition complex subunit 4 × 1 (P54791) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.98 Å

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.

25 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ORC1_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain A; PDBConstruct 1–914; UniProt 1–914

Origin recognition complex subunit 3

Saccharomyces cerevisiae S288C

UniProt P54790

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–DNA Heteromer Protein × 6 DNA 2 PDB declaration: octameric(8) Consistent with all polymer counts Chain C; UniProt 1–616 Not recorded Origin recognition complex subunit 2 × 1 (P32833) Origin recognition complex subunit 5 × 1 (P50874) Origin recognition complex subunit 6 × 1 (P38826) DNA (35-MER) × 1 DNA (34-MER) × 1 Origin recognition complex subunit 1 × 1 (P54784) Origin recognition complex subunit 4 × 1 (P54791) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.98 Å

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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ORC3_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain C; PDBConstruct 1–616; UniProt 1–616

Origin recognition complex subunit 4

Saccharomyces cerevisiae S288C

UniProt P54791

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–DNA Heteromer Protein × 6 DNA 2 PDB declaration: octameric(8) Consistent with all polymer counts Chain D; UniProt 1–529 Not recorded Origin recognition complex subunit 2 × 1 (P32833) Origin recognition complex subunit 5 × 1 (P50874) Origin recognition complex subunit 6 × 1 (P38826) DNA (35-MER) × 1 DNA (34-MER) × 1 Origin recognition complex subunit 1 × 1 (P54784) Origin recognition complex subunit 3 × 1 (P54790) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.98 Å

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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ORC4_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain D; PDBConstruct 1–529; UniProt 1–529

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 8zp5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8zp5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8zp5
Deposition date deposition_date2024-05-29
最后修订 last_revision2025-04-16
Structure title titleCryo-EM structure of origin recognition complex (Orc5 basic patch mutations) with ARS1 DNA bound
Keywords keywordsREPLICATION; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.77
Radius of gyration Rg (electron density) rg_electron45.92
Forward intensity I(0) i01400190000.00
Molecular weight molecular_weight306380.0 kDa
Excluded volume excluded_volume381450 ų
Envelope volume envelope_volume511000 ų
Hydration-shell volume shell_volume90315 ų
Envelope diameter envelope_diameter171.8
Shell Rg shell_rg51.99
Envelope Rg envelope_rg45.77
Shape Rg shape_rg45.95
Total Rg total_rg46.06
Total atoms total_atoms21482
Residues n_residues2515
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 dmax156.9
Rg (real space) rg_real45.72
Rg uncertainty (real space) rg_real_error1.34
I(0) (real space) i0_real1.4000e+09
I(0) uncertainty (real space) i0_real_error2.5960e+07
Rg (reciprocal space) rg_reciprocal45.77
I(0) (reciprocal space) i0_reciprocal1400000000.0000
Solution quality estimate total_estimate0.8654
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary152.3
Skewness Skewness skewness0.366
Kurtosis Kurtosis kurtosis-0.203
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha228100000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.784; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.907

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)