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1a5e

SOLUTION NMR STRUCTURE OF TUMOR SUPPRESSOR P16INK4A, 18 STRUCTURES

Method: SOLUTION NMR Dmax: 51.8 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

TUMOR SUPPRESSOR P16INK4A

Homo sapiens

UniProt P42771

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 1–156 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions：pH 7.5；293 K；Ionic strength (raw mmCIF value) CA. 0；Pressure NO NMR sample composition：H2O AND D2O Resolution not provided

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.

Other PDB Difference from Current Entry 1A5E Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BI7 MECHANISM OF G1 CYCLIN DEPENDENT KINASE INHIBITION FROM THE STRUCTURE OF THE CDK6-P16INK4A TUMOR SUPPRESSOR COMPLEX Deposited 1998-06-22 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–156（156 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 3.40 Å R-free 0.330
1DC2 SOLUTION NMR STRUCTURE OF TUMOR SUPPRESSOR P16INK4A, 20 STRUCTURES Deposited 1999-11-04 Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–156（156 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.5；293 K；Ionic strength (raw mmCIF value) 0；Pressure AMBIENT
NMR sample composition 0.2-0.4 MM P16INK4A U-15N,13C; 4 MM HEPES, 1 MM DTT, 5 UM EDTA; 95% H2O, 5% D2O
NMR sample composition 0.2-0.4 MM P16INK4A U-15N; 4 MM HEPES, 1 MM DTT, 5 UM EDTA; 95% H2O, 5% D2O
NMR sample composition 0.2-0.4 MM P16INK4A; 4 MM HEPES, 1 MM DTT, 5 UM EDTA; 95% H2O, 5% D2O
Resolution not provided
2A5E SOLUTION NMR STRUCTURE OF TUMOR SUPPRESSOR P16INK4A, RESTRAINED MINIMIZED MEAN STRUCTURE Deposited 1998-02-13 Parsed fields agree Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–156（156 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.5；293 K；Ionic strength (raw mmCIF value) CA. 0；Pressure NO
NMR sample composition H2O AND D2O
Resolution not provided
7OZT Nanobodies restore stability to cancer-associated mutants of tumor suppressor protein p16INK4a Deposited 2021-06-28 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain BBB 1–156（156 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；Molecular Dimensions Morpheus screen condition G4
Resolution 1.74 Å R-free 0.209

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDN2A_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–156； UniProt 1–156

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 1a5e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a5e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1a5e
Deposition date deposition_date1998-02-13
Structure title titleSOLUTION NMR STRUCTURE OF TUMOR SUPPRESSOR P16INK4A, 18 STRUCTURES
Keywords keywordsCELL CYCLE, ANTI-ONCOGENE, ANK REPEAT; ANTI-ONCOGENE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier19.01 Å
Radius of gyration Rg (electron density) rg_electron18.64 Å
Forward intensity I(0) i01423260000.00
Molecular weight molecular_weight297500.0 kDa
Excluded volume excluded_volume364530 ų
Envelope volume envelope_volume93815 ų
Hydration-shell volume shell_volume28206 ų
Envelope diameter envelope_diameter109.2 Å
Shell Rg shell_rg35.08 Å
Envelope Rg envelope_rg29.68 Å
Shape Rg shape_rg18.62 Å
Total Rg total_rg19.10 Å
Total atoms total_atoms41418
Residues n_residues2808
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax51.8 Å
Rg (real space) rg_real17.60 Å
Rg uncertainty (real space) rg_real_error0.10 Å
I(0) (real space) i0_real1.3520e+09
I(0) uncertainty (real space) i0_real_error1.2410e+07
Rg (reciprocal space) rg_reciprocal19.35 Å
I(0) (reciprocal space) i0_reciprocal1423000000.0000
Solution quality estimate total_estimate0.6750
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary18.7 Å
Skewness Skewness skewness0.469
Kurtosis Kurtosis kurtosis-0.312
Angular range angular_range— – 0.4200 Å−1
Current regularization parameter α current_alpha3.2480
Highest regularization parameter α highest_alpha1348000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.009; Oscil: 0.939; Stabil: 0.991; Sysdev: 0.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1a5ea_
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_id1a5eA00
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
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8. Citations (1)

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9. Files and Curves (10)