9ja0

The capsid protein of HIV 1

Method: ELECTRON MICROSCOPY Dmax: 144.9 Å Quality: GOOD

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

Capsid protein p24

Human immunodeficiency virus 1

UniProt P0C6F2

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 homooligomer Homooligomer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 133–353 Chain B; UniProt 133–353 Chain C; UniProt 133–353 Chain D; UniProt 133–353 Chain E; UniProt 133–353 Chain F; UniProt 133–353 Chain G; UniProt 133–353 Chain H; UniProt 133–353 Chain I; UniProt 133–353 Chain J; UniProt 133–353 Chain K; UniProt 133–353 Chain L; UniProt 133–353 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.14 Å

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.

17 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POL_HV1LW
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–221; UniProt 133–353 Author chain B; PDBConstruct 1–221; UniProt 133–353 Author chain C; PDBConstruct 1–221; UniProt 133–353 Author chain D; PDBConstruct 1–221; UniProt 133–353 Author chain E; PDBConstruct 1–221; UniProt 133–353 Author chain F; PDBConstruct 1–221; UniProt 133–353 Author chain G; PDBConstruct 1–221; UniProt 133–353 Author chain H; PDBConstruct 1–221; UniProt 133–353 Author chain I; PDBConstruct 1–221; UniProt 133–353 Author chain J; PDBConstruct 1–221; UniProt 133–353 Author chain K; PDBConstruct 1–221; UniProt 133–353 Author chain L; PDBConstruct 1–221; UniProt 133–353

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 9ja0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ja0
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9ja0
Deposition date deposition_date2024-08-23
Structure title titleThe capsid protein of HIV 1
Keywords keywordsHIV 1, Capsid protein, Di-Hexamer, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.58
Radius of gyration Rg (electron density) rg_electron45.12
Forward intensity I(0) i01207460000.00
Molecular weight molecular_weight281480.0 kDa
Excluded volume excluded_volume350020 ų
Envelope volume envelope_volume497260 ų
Hydration-shell volume shell_volume89415 ų
Envelope diameter envelope_diameter145.0
Shell Rg shell_rg51.51
Envelope Rg envelope_rg44.26
Shape Rg shape_rg45.14
Total Rg total_rg45.32
Total atoms total_atoms19716
Residues n_residues2628
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 dmax144.9
Rg (real space) rg_real45.34
Rg uncertainty (real space) rg_real_error0.94
I(0) (real space) i0_real1.2070e+09
I(0) uncertainty (real space) i0_real_error2.0660e+07
Rg (reciprocal space) rg_reciprocal45.58
I(0) (reciprocal space) i0_reciprocal1208000000.0000
Solution quality estimate total_estimate0.8775
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.0
Skewness Skewness skewness0.183
Kurtosis Kurtosis kurtosis-0.387
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha157100000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.883; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.775

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)