8zp4

Cryo-EM structure of origin recognition complex (Orc1 to 5) with ARS1 DNA bound

Method: ELECTRON MICROSCOPY Dmax: 145.8 Å Quality: GOOD

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

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 × 5 DNA 2 PDB declaration: heptameric(7) Consistent with all polymer counts Chain A; UniProt 1–914 Not recorded Origin recognition complex subunit 2 × 1 (P32833) Origin recognition complex subunit 3 × 1 (P54790) Origin recognition complex subunit 4 × 1 (P54791) DNA (31-MER) × 1 DNA (31-MER) × 1 Origin recognition complex subunit 5 × 1 (P50874) 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 3.33 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–914; UniProt 1–914

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 × 5 DNA 2 PDB declaration: heptameric(7) Consistent with all polymer counts Chain B; UniProt 1–620 Not recorded Origin recognition complex subunit 1 × 1 (P54784) Origin recognition complex subunit 3 × 1 (P54790) Origin recognition complex subunit 4 × 1 (P54791) DNA (31-MER) × 1 DNA (31-MER) × 1 Origin recognition complex subunit 5 × 1 (P50874) 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 3.33 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–620; UniProt 1–620

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 × 5 DNA 2 PDB declaration: heptameric(7) Consistent with all polymer counts Chain C; UniProt 1–616 Not recorded Origin recognition complex subunit 1 × 1 (P54784) Origin recognition complex subunit 2 × 1 (P32833) Origin recognition complex subunit 4 × 1 (P54791) DNA (31-MER) × 1 DNA (31-MER) × 1 Origin recognition complex subunit 5 × 1 (P50874) 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 3.33 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 3
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 × 5 DNA 2 PDB declaration: heptameric(7) Consistent with all polymer counts Chain D; UniProt 1–529 Not recorded Origin recognition complex subunit 1 × 1 (P54784) Origin recognition complex subunit 2 × 1 (P32833) Origin recognition complex subunit 3 × 1 (P54790) DNA (31-MER) × 1 DNA (31-MER) × 1 Origin recognition complex subunit 5 × 1 (P50874) 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 3.33 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 4
Chains and sequence ranges Author chain D; PDBConstruct 1–529; UniProt 1–529

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 × 5 DNA 2 PDB declaration: heptameric(7) Consistent with all polymer counts Chain E; UniProt 1–479 Not recorded Origin recognition complex subunit 1 × 1 (P54784) Origin recognition complex subunit 2 × 1 (P32833) Origin recognition complex subunit 3 × 1 (P54790) Origin recognition complex subunit 4 × 1 (P54791) DNA (31-MER) × 1 DNA (31-MER) × 1 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 3.33 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 7
Chains and sequence ranges Author chain E; PDBConstruct 1–479; UniProt 1–479

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 8zp4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8zp4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8zp4
Deposition date deposition_date2024-05-29
最后修订 last_revision2025-04-16
Structure title titleCryo-EM structure of origin recognition complex (Orc1 to 5) with ARS1 DNA bound
Keywords keywordsorigin recognition complex, REPLICATION; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.89
Radius of gyration Rg (electron density) rg_electron43.91
Forward intensity I(0) i01222790000.00
Molecular weight molecular_weight285560.0 kDa
Excluded volume excluded_volume355550 ų
Envelope volume envelope_volume476540 ų
Hydration-shell volume shell_volume87289 ų
Envelope diameter envelope_diameter157.8
Shell Rg shell_rg51.05
Envelope Rg envelope_rg43.70
Shape Rg shape_rg43.96
Total Rg total_rg44.05
Total atoms total_atoms20029
Residues n_residues2348
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 dmax145.8
Rg (real space) rg_real43.77
Rg uncertainty (real space) rg_real_error1.05
I(0) (real space) i0_real1.2230e+09
I(0) uncertainty (real space) i0_real_error2.0660e+07
Rg (reciprocal space) rg_reciprocal43.89
I(0) (reciprocal space) i0_reciprocal1223000000.0000
Solution quality estimate total_estimate0.8758
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary52.6
Skewness Skewness skewness0.304
Kurtosis Kurtosis kurtosis-0.248
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha239100000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.830; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.898

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)