8unj

Atomic model of the human CTF18-RFC alone in the apo state (State 1)

Method: ELECTRON MICROSCOPY Dmax: 117.4 Å Quality: EXCELLENT

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

Chromosome transmission fidelity protein 18 homolog

Homo sapiens

UniProt Q8WVB6

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 1–975 Not recorded Replication factor C subunit 2 × 1 (P35250) Replication factor C subunit 5 × 1 (P40937) Replication factor C subunit 4 × 1 (P35249) Replication factor C subunit 3 × 1 (P40938) MG MAGNESIUM ION × 3 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.35 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CTF18_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–975; UniProt 1–975

Replication factor C subunit 2

Homo sapiens

UniProt P35250

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 1–354 Not recorded Chromosome transmission fidelity protein 18 homolog × 1 (Q8WVB6) Replication factor C subunit 5 × 1 (P40937) Replication factor C subunit 4 × 1 (P35249) Replication factor C subunit 3 × 1 (P40938) MG MAGNESIUM ION × 3 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.35 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 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RFC2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–354; UniProt 1–354

Replication factor C subunit 5

Homo sapiens

UniProt P40937

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 1–340 Not recorded Chromosome transmission fidelity protein 18 homolog × 1 (Q8WVB6) Replication factor C subunit 2 × 1 (P35250) Replication factor C subunit 4 × 1 (P35249) Replication factor C subunit 3 × 1 (P40938) MG MAGNESIUM ION × 3 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.35 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 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RFC5_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–340; UniProt 1–340

Replication factor C subunit 4

Homo sapiens

UniProt P35249

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 1–363 Not recorded Chromosome transmission fidelity protein 18 homolog × 1 (Q8WVB6) Replication factor C subunit 2 × 1 (P35250) Replication factor C subunit 5 × 1 (P40937) Replication factor C subunit 3 × 1 (P40938) MG MAGNESIUM ION × 3 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.35 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 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RFC4_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–363; UniProt 1–363

Replication factor C subunit 3

Homo sapiens

UniProt P40938

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 1–356 Not recorded Chromosome transmission fidelity protein 18 homolog × 1 (Q8WVB6) Replication factor C subunit 2 × 1 (P35250) Replication factor C subunit 5 × 1 (P40937) Replication factor C subunit 4 × 1 (P35249) MG MAGNESIUM ION × 3 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.35 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 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RFC3_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–356; UniProt 1–356

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 8unj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8unj
Deposition date deposition_date2023-10-19
Structure title titleAtomic model of the human CTF18-RFC alone in the apo state (State 1)
Keywords keywordsDNA clamp loader complex, REPLICATION; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.86
Radius of gyration Rg (electron density) rg_electron37.23
Forward intensity I(0) i0441240000.00
Molecular weight molecular_weight170290.0 kDa
Excluded volume excluded_volume213500 ų
Envelope volume envelope_volume288340 ų
Hydration-shell volume shell_volume62554 ų
Envelope diameter envelope_diameter123.5
Shell Rg shell_rg44.95
Envelope Rg envelope_rg36.73
Shape Rg shape_rg37.25
Total Rg total_rg37.64
Total atoms total_atoms11916
Residues n_residues1493
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 dmax117.4
Rg (real space) rg_real37.65
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real4.4120e+08
I(0) uncertainty (real space) i0_real_error6.8820e+06
Rg (reciprocal space) rg_reciprocal37.79
I(0) (reciprocal space) i0_reciprocal441300000.0000
Solution quality estimate total_estimate0.9038
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.7
Skewness Skewness skewness0.130
Kurtosis Kurtosis kurtosis-0.589
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha70450000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.948; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.916

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)