7cng

Structure of CDK5R1 bound FEM1B

Method: X-RAY DIFFRACTION Dmax: 115.7 Å Quality: GOOD

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

Protein fem-1 homolog B,Peptide from Cyclin-dependent kinase 5 activator 1

Homo sapiens

UniProt Q15078

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 298–307 Not recorded SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;1.6M Magnesium sulfate hydrate, 0.1M BIS-TRIS propane pH 6.7 Resolution 3.49 Å R-free 0.267
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 298–307 Not recorded SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;1.6M Magnesium sulfate hydrate, 0.1M BIS-TRIS propane pH 6.7 Resolution 3.49 Å R-free 0.267

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.

10 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CD5R1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 348–357; UniProt 298–307 Author chain B; PDBConstruct 348–357; UniProt 298–307

Protein fem-1 homolog B,Peptide from Cyclin-dependent kinase 5 activator 1

Homo sapiens

UniProt Q9UK73

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–337 Not recorded SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;1.6M Magnesium sulfate hydrate, 0.1M BIS-TRIS propane pH 6.7 Resolution 3.49 Å R-free 0.267
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–337 Not recorded SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;1.6M Magnesium sulfate hydrate, 0.1M BIS-TRIS propane pH 6.7 Resolution 3.49 Å R-free 0.267

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.

30 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FEM1B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–339; UniProt 1–337 Author chain B; PDBConstruct 3–339; UniProt 1–337

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 7cng

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7cng
Deposition date deposition_date2020-07-31
Structure title titleStructure of CDK5R1 bound FEM1B
Keywords keywordsubiquitination, E3 ligase, degron, PEPTIDE BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.92
Radius of gyration Rg (electron density) rg_electron32.84
Forward intensity I(0) i085325800.00
Molecular weight molecular_weight72870.0 kDa
Excluded volume excluded_volume90985 ų
Envelope volume envelope_volume121610 ų
Hydration-shell volume shell_volume32121 ų
Envelope diameter envelope_diameter120.8
Shell Rg shell_rg38.08
Envelope Rg envelope_rg32.38
Shape Rg shape_rg32.85
Total Rg total_rg33.26
Total atoms total_atoms5124
Residues n_residues686
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 dmax115.7
Rg (real space) rg_real33.10
Rg uncertainty (real space) rg_real_error1.10
I(0) (real space) i0_real8.5330e+07
I(0) uncertainty (real space) i0_real_error1.4340e+06
Rg (reciprocal space) rg_reciprocal33.03
I(0) (reciprocal space) i0_reciprocal85320000.0000
Solution quality estimate total_estimate0.8588
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.0
Skewness Skewness skewness0.403
Kurtosis Kurtosis kurtosis-0.331
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14110000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.809; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.804; Smooth: 0.928

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)