9iin

Structure of CTF18-PCNA with ATP and Mg2+

Method: ELECTRON MICROSCOPY Dmax: 132.5 Å Quality: GOOD

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 2–975 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) Proliferating cell nuclear antigen × 3 (P12004) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;50 mM Tris-HCl, 200 mM NaCl, 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 39–1012; UniProt 2–975

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 × 8 PDB declaration: octameric(8) 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) Proliferating cell nuclear antigen × 3 (P12004) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;50 mM Tris-HCl, 200 mM NaCl, 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 × 8 PDB declaration: octameric(8) 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) Proliferating cell nuclear antigen × 3 (P12004) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;50 mM Tris-HCl, 200 mM NaCl, 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 × 8 PDB declaration: octameric(8) 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) Proliferating cell nuclear antigen × 3 (P12004) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;50 mM Tris-HCl, 200 mM NaCl, 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 × 8 PDB declaration: octameric(8) 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) Proliferating cell nuclear antigen × 3 (P12004) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;50 mM Tris-HCl, 200 mM NaCl, 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 7–362; UniProt 1–356

Proliferating cell nuclear antigen

Homo sapiens

UniProt P12004

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain F; UniProt 1–261 Chain G; UniProt 1–261 Chain H; UniProt 1–261 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) Replication factor C subunit 3 × 1 (P40938) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;50 mM Tris-HCl, 200 mM NaCl, 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

101 other PDB entries and 126 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PCNA_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 7–267; UniProt 1–261 Author chain G; PDBConstruct 7–267; UniProt 1–261 Author chain H; PDBConstruct 7–267; UniProt 1–261

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 9iin

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9iin
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9iin
Deposition date deposition_date2024-06-20
Structure title titleStructure of CTF18-PCNA with ATP and Mg2+
Keywords keywordsCTF18-RFC, human clamp loader; PCNA, sliding clamp; complex, ATP, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.81
Radius of gyration Rg (electron density) rg_electron43.00
Forward intensity I(0) i01163470000.00
Molecular weight molecular_weight282380.0 kDa
Excluded volume excluded_volume354180 ų
Envelope volume envelope_volume490920 ų
Hydration-shell volume shell_volume91093 ų
Envelope diameter envelope_diameter141.2
Shell Rg shell_rg51.87
Envelope Rg envelope_rg41.40
Shape Rg shape_rg43.01
Total Rg total_rg43.34
Total atoms total_atoms19773
Residues n_residues2504
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 dmax132.5
Rg (real space) rg_real43.47
Rg uncertainty (real space) rg_real_error0.73
I(0) (real space) i0_real1.1630e+09
I(0) uncertainty (real space) i0_real_error2.0030e+07
Rg (reciprocal space) rg_reciprocal43.81
I(0) (reciprocal space) i0_reciprocal1164000000.0000
Solution quality estimate total_estimate0.8968
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.9
Skewness Skewness skewness0.008
Kurtosis Kurtosis kurtosis-0.544
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha127500000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.920; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.954; Smooth: 0.939

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (2)

9. Files and Curves (10)