7jpr

ORC-OPEN: Human Origin Recognition Complex (ORC) in an open conformation

Method: ELECTRON MICROSCOPY Dmax: 161.3 Å Quality: GOOD

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

Origin recognition complex subunit 1

Homo sapiens

UniProt Q13415

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 471–861 Not recorded Origin recognition complex subunit 2 × 1 (Q13416) Origin recognition complex subunit 3 × 1 (Q9UBD5) Origin recognition complex subunit 4 × 1 (O43929) Origin recognition complex subunit 5 × 1 (O43913) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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.

12 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ORC1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–392; UniProt 471–861

Origin recognition complex subunit 2

Homo sapiens

UniProt Q13416

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 1–577 Not recorded Origin recognition complex subunit 1 × 1 (Q13415) Origin recognition complex subunit 3 × 1 (Q9UBD5) Origin recognition complex subunit 4 × 1 (O43929) Origin recognition complex subunit 5 × 1 (O43913) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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.

15 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ORC2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–577; UniProt 1–577

Origin recognition complex subunit 3

Homo sapiens

UniProt Q9UBD5

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 1–712 Not recorded Origin recognition complex subunit 1 × 1 (Q13415) Origin recognition complex subunit 2 × 1 (Q13416) Origin recognition complex subunit 4 × 1 (O43929) Origin recognition complex subunit 5 × 1 (O43913) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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.

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

View Construct and Data Evidence
UniProt name ORC3_HUMAN
Isoform Q9UBD5-2
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–712; UniProt 1–712

Origin recognition complex subunit 4

Homo sapiens

UniProt O43929

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 1–436 Not recorded Origin recognition complex subunit 1 × 1 (Q13415) Origin recognition complex subunit 2 × 1 (Q13416) Origin recognition complex subunit 3 × 1 (Q9UBD5) Origin recognition complex subunit 5 × 1 (O43913) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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.

14 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ORC4_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–436; UniProt 1–436

Origin recognition complex subunit 5

Homo sapiens

UniProt O43913

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 1–435 Not recorded Origin recognition complex subunit 1 × 1 (Q13415) Origin recognition complex subunit 2 × 1 (Q13416) Origin recognition complex subunit 3 × 1 (Q9UBD5) Origin recognition complex subunit 4 × 1 (O43929) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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.

14 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ORC5_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–435; UniProt 1–435

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 7jpr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7jpr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7jpr
Deposition date deposition_date2020-08-09
Structure title titleORC-OPEN: Human Origin Recognition Complex (ORC) in an open conformation
Keywords keywordsreplication, AAA+, ORC, DNA-binding; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier46.96
Radius of gyration Rg (electron density) rg_electron46.56
Forward intensity I(0) i0790073000.00
Molecular weight molecular_weight237850.0 kDa
Excluded volume excluded_volume300210 ų
Envelope volume envelope_volume437890 ų
Hydration-shell volume shell_volume78861 ų
Envelope diameter envelope_diameter167.5
Shell Rg shell_rg50.80
Envelope Rg envelope_rg45.31
Shape Rg shape_rg46.56
Total Rg total_rg46.75
Total atoms total_atoms16737
Residues n_residues2045
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 dmax161.3
Rg (real space) rg_real46.98
Rg uncertainty (real space) rg_real_error1.41
I(0) (real space) i0_real7.9010e+08
I(0) uncertainty (real space) i0_real_error1.4980e+07
Rg (reciprocal space) rg_reciprocal46.96
I(0) (reciprocal space) i0_reciprocal790100000.0000
Solution quality estimate total_estimate0.8772
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.2
Skewness Skewness skewness0.342
Kurtosis Kurtosis kurtosis-0.340
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha95250000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.844; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.867

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7jprD01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id7jprE01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)