2od8

Structure of a peptide derived from Cdc9 bound to PCNA

Method: X-RAY DIFFRACTION Dmax: 68.8 Å Quality: GOOD

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

Proliferating cell nuclear antigen

Saccharomyces cerevisiae

UniProt P15873

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–258 Not recorded DNA ligase I, mitochondrial precursor × 3 (P04819) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;294 K;1.6 M (NH4)2SO4, Sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 2.80 Å R-free 0.285

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.

55 other PDB entries and 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PCNA_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–258; UniProt 1–258

DNA ligase I, mitochondrial precursor

OrganismNot specified

UniProt P04819

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 32–53 Fragment:Residues 32-53 Proliferating cell nuclear antigen × 3 (P15873) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;294 K;1.6 M (NH4)2SO4, Sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 2.80 Å R-free 0.285

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name DNLI_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–22; UniProt 32–53

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 2od8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2od8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2od8
Deposition date deposition_date2006-12-21
Structure title titleStructure of a peptide derived from Cdc9 bound to PCNA
Keywords keywordshomotrimer, PCNA-peptide complex, PCNA, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.32
Radius of gyration Rg (electron density) rg_electron20.03
Forward intensity I(0) i014640000.00
Molecular weight molecular_weight29801.0 kDa
Excluded volume excluded_volume37813 ų
Envelope volume envelope_volume45593 ų
Hydration-shell volume shell_volume19372 ų
Envelope diameter envelope_diameter69.3
Shell Rg shell_rg26.15
Envelope Rg envelope_rg20.38
Shape Rg shape_rg19.99
Total Rg total_rg21.10
Total atoms total_atoms2095
Residues n_residues266
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 dmax68.8
Rg (real space) rg_real21.29
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real1.4640e+07
I(0) uncertainty (real space) i0_real_error2.0360e+05
Rg (reciprocal space) rg_reciprocal21.30
I(0) (reciprocal space) i0_reciprocal14640000.0000
Solution quality estimate total_estimate0.8915
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.3
Skewness Skewness skewness0.300
Kurtosis Kurtosis kurtosis-0.421
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2492000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.866; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2od8a1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.131 — DNA clamp
Superfamily Superfamily superfamilyd.131.1 — DNA clamp
Family Family familyd.131.1.2 — DNA polymerase processivity factor
Domain ID domain_idd2od8a2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.131 — DNA clamp
Superfamily Superfamily superfamilyd.131.1 — DNA clamp
Family Family familyd.131.1.2 — DNA polymerase processivity factor

CATH v4.4 (1 domains)

Domain ID domain_id2od8A00
Class class3 — Alpha Beta
Architecture architecture70 — Box
Topology topology10 — Proliferating Cell Nuclear Antigen
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)