7efa

Crystal structure of the complex between the C-terminal domain of mouse MUTYH and human PCNA

Method: X-RAY DIFFRACTION Dmax: 83.8 Å Quality: EXCELLENT

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

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–261 Not recorded Adenine DNA glycosylase × 3 (Q99P21) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;PEG8000, imidazole Resolution 2.70 Å R-free 0.286

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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–261; UniProt 1–261

Adenine DNA glycosylase

Mus musculus

UniProt Q99P21

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 331–515 Not recorded Proliferating cell nuclear antigen × 3 (P12004) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;PEG8000, imidazole Resolution 2.70 Å R-free 0.286

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MUTYH_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 5–189; UniProt 331–515

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 7efa

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7efa
Deposition date deposition_date2021-03-21
Structure title titleCrystal structure of the complex between the C-terminal domain of mouse MUTYH and human PCNA
Keywords keywordsDNA replication, DNA repair, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.36
Radius of gyration Rg (electron density) rg_electron25.18
Forward intensity I(0) i029944900.00
Molecular weight molecular_weight40555.0 kDa
Excluded volume excluded_volume50189 ų
Envelope volume envelope_volume68763 ų
Hydration-shell volume shell_volume23843 ų
Envelope diameter envelope_diameter86.8
Shell Rg shell_rg31.33
Envelope Rg envelope_rg25.26
Shape Rg shape_rg25.21
Total Rg total_rg25.86
Total atoms total_atoms2851
Residues n_residues401
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 dmax83.8
Rg (real space) rg_real26.38
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real2.9940e+07
I(0) uncertainty (real space) i0_real_error4.4170e+05
Rg (reciprocal space) rg_reciprocal26.38
I(0) (reciprocal space) i0_reciprocal29940000.0000
Solution quality estimate total_estimate0.9018
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.1
Skewness Skewness skewness0.303
Kurtosis Kurtosis kurtosis-0.559
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8116000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.960; Smooth: 0.982

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_idd7efaa1
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_idd7efaa2
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_id7efaB01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology79 — Nucleoside Triphosphate Pyrophosphohydrolase
Homologous superfamily homologous superfamily10 — Nucleoside Triphosphate Pyrophosphohydrolase

8. Citations (1)

9. Files and Curves (10)