1bd8

STRUCTURE OF CDK INHIBITOR P19INK4D

Method: X-RAY DIFFRACTION Dmax: 61.6 Å Quality: REASONABLE

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

P19INK4D CDK4/6 INHIBITOR

Homo sapiens

UniProt P55273

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 7–162 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;277 K;PROTEIN WAS CRYSTALLIZED FROM 35% PEG 4000, 200 MM MGSO4 AND 200 MM TRIS/HCL PH 8.5, SITTING DROP METHOD, AT 4 DEG. C., vapor diffusion - sitting drop, temperature 277K Resolution 1.80 Å R-free 0.260

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDN2D_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–156; UniProt 7–162

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 1bd8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1bd8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1bd8
Deposition date deposition_date1998-05-12
Structure title titleSTRUCTURE OF CDK INHIBITOR P19INK4D
Keywords keywordsTUMOR SUPPRESSOR, CDK4/6 INHIBITOR, ANKYRIN MOTIF; TUMOR SUPPRESSOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.88
Radius of gyration Rg (electron density) rg_electron16.96
Forward intensity I(0) i05611940.00
Molecular weight molecular_weight16601.0 kDa
Excluded volume excluded_volume20560 ų
Envelope volume envelope_volume24059 ų
Hydration-shell volume shell_volume12806 ų
Envelope diameter envelope_diameter61.4
Shell Rg shell_rg21.80
Envelope Rg envelope_rg17.34
Shape Rg shape_rg16.93
Total Rg total_rg17.86
Total atoms total_atoms1168
Residues n_residues156
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 dmax61.6
Rg (real space) rg_real17.98
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real5.6120e+06
I(0) uncertainty (real space) i0_real_error7.1410e+04
Rg (reciprocal space) rg_reciprocal17.97
I(0) (reciprocal space) i0_reciprocal5612000.0000
Solution quality estimate total_estimate0.6583
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.3
Skewness Skewness skewness0.500
Kurtosis Kurtosis kurtosis-0.248
Angular range angular_range— – 0.4450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2164000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.694; Stabil: 1.000; Sysdev: 0.227; Positv: 1.000; Valcen: 0.909; Smooth: 0.882

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1bd8a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.211 — beta-hairpin-alpha-hairpin repeat
Superfamily Superfamily superfamilyd.211.1 — Ankyrin repeat
Family Family familyd.211.1.1 — Ankyrin repeat

CATH v4.4 (1 domains)

Domain ID domain_id1bd8A00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily20 — Ankyrin repeat-containing domain

8. Citations (2)

9. Files and Curves (10)