7smc

p107 pocket domain complexed with ARID4A peptide

Method: X-RAY DIFFRACTION Dmax: 89.0 Å Quality: EXCELLENT

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

Retinoblastoma-like protein 1

Homo sapiens

UniProt P28749

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 391–601 Chain A; UniProt 780–887 Chain A; UniProt 924–972 Fragment:UNP residues 391-601,780-887,924-972 AT-rich interactive domain-containing protein 4A × 1 (P29374) SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;100 mM MES, pH 6.5, 4% PEG400, 1.6 M ammonium sulfate Resolution 2.70 Å R-free 0.298
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 391–601 Chain C; UniProt 780–887 Chain C; UniProt 924–972 Fragment:UNP residues 391-601,780-887,924-972 AT-rich interactive domain-containing protein 4A × 1 (P29374) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;100 mM MES, pH 6.5, 4% PEG400, 1.6 M ammonium sulfate Resolution 2.70 Å R-free 0.298

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 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBL1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–214; UniProt 391–601 Author chain A; PDBConstruct 215–322; UniProt 780–887 Author chain A; PDBConstruct 323–371; UniProt 924–972 Author chain C; PDBConstruct 4–214; UniProt 391–601 Author chain C; PDBConstruct 215–322; UniProt 780–887 Author chain C; PDBConstruct 323–371; UniProt 924–972

AT-rich interactive domain-containing protein 4A

OrganismNot specified

UniProt P29374

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 953–967 Fragment:UNP residues 953-967 Retinoblastoma-like protein 1 × 1 (P28749) SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;100 mM MES, pH 6.5, 4% PEG400, 1.6 M ammonium sulfate Resolution 2.70 Å R-free 0.298
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 953–967 Fragment:UNP residues 953-967 Retinoblastoma-like protein 1 × 1 (P28749) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;100 mM MES, pH 6.5, 4% PEG400, 1.6 M ammonium sulfate Resolution 2.70 Å R-free 0.298

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.

6 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARI4A_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–15; UniProt 953–967 Author chain D; PDBConstruct 1–15; UniProt 953–967

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 7smc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7smc
Deposition date deposition_date2021-10-25
Structure title titlep107 pocket domain complexed with ARID4A peptide
Keywords keywordsTranscription, cyclin box pocket transcriptional regulator, cell cycle; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.43
Radius of gyration Rg (electron density) rg_electron28.24
Forward intensity I(0) i0103221000.00
Molecular weight molecular_weight81345.0 kDa
Excluded volume excluded_volume102440 ų
Envelope volume envelope_volume128700 ų
Hydration-shell volume shell_volume37374 ų
Envelope diameter envelope_diameter93.4
Shell Rg shell_rg35.99
Envelope Rg envelope_rg28.03
Shape Rg shape_rg28.21
Total Rg total_rg29.12
Total atoms total_atoms5719
Residues n_residues705
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 dmax89.0
Rg (real space) rg_real29.27
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real1.0320e+08
I(0) uncertainty (real space) i0_real_error1.4140e+06
Rg (reciprocal space) rg_reciprocal29.34
I(0) (reciprocal space) i0_reciprocal103200000.0000
Solution quality estimate total_estimate0.9080
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.2
Skewness Skewness skewness0.106
Kurtosis Kurtosis kurtosis-0.522
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24650000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.952; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.961

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)