8uii

Cryo-EM map of human clamp-clamp loader ATAD5-RFC-closed PCNA complex in intermediate state 1

Method: ELECTRON MICROSCOPY Dmax: 141.6 Å Quality: GOOD

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

ATPase family AAA domain-containing protein 5

Homo sapiens

UniProt Q96QE3

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 1–1844 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) MG MAGNESIUM ION × 4 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.04 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATAD5_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1844; UniProt 1–1844

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 ATPase family AAA domain-containing protein 5 × 1 (Q96QE3) 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) MG MAGNESIUM ION × 4 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.04 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 ATPase family AAA domain-containing protein 5 × 1 (Q96QE3) 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) MG MAGNESIUM ION × 4 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.04 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 ATPase family AAA domain-containing protein 5 × 1 (Q96QE3) 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) MG MAGNESIUM ION × 4 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.04 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 ATPase family AAA domain-containing protein 5 × 1 (Q96QE3) 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) MG MAGNESIUM ION × 4 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.04 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

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 ATPase family AAA domain-containing protein 5 × 1 (Q96QE3) 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 × 4 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.04 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 1–261; UniProt 1–261 Author chain G; PDBConstruct 1–261; UniProt 1–261 Author chain H; PDBConstruct 1–261; 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 8uii

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8uii
Deposition date deposition_date2023-10-10
Structure title titleCryo-EM map of human clamp-clamp loader ATAD5-RFC-closed PCNA complex in intermediate state 1
Keywords keywordsAAA ATPase, Clamp unloader, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.31
Radius of gyration Rg (electron density) rg_electron44.55
Forward intensity I(0) i01400420000.00
Molecular weight molecular_weight310080.0 kDa
Excluded volume excluded_volume388320 ų
Envelope volume envelope_volume539430 ų
Hydration-shell volume shell_volume95463 ų
Envelope diameter envelope_diameter146.3
Shell Rg shell_rg53.66
Envelope Rg envelope_rg43.70
Shape Rg shape_rg44.55
Total Rg total_rg44.90
Total atoms total_atoms21704
Residues n_residues2743
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 dmax141.6
Rg (real space) rg_real45.02
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real1.4000e+09
I(0) uncertainty (real space) i0_real_error2.6940e+07
Rg (reciprocal space) rg_reciprocal45.30
I(0) (reciprocal space) i0_reciprocal1401000000.0000
Solution quality estimate total_estimate0.8973
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.6
Skewness Skewness skewness0.109
Kurtosis Kurtosis kurtosis-0.532
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha179000000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.919; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.926

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)