7ovr

Mature HIV-1 matrix structure

Method: ELECTRON MICROSCOPY Dmax: 191.8 Å Quality: GOOD

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

HIV-1 matrix

Human immunodeficiency virus 1

UniProt B6DRA0

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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain A; UniProt 2–116 Chain B; UniProt 2–116 Chain C; UniProt 2–116 Chain D; UniProt 2–116 Chain E; UniProt 2–116 Chain F; UniProt 2–116 Chain H; UniProt 2–116 Chain I; UniProt 2–116 Chain J; UniProt 2–116 Chain O; UniProt 2–116 Chain P; UniProt 2–116 Chain Q; UniProt 2–116 Chain R; UniProt 2–116 Chain S; UniProt 2–116 Chain U; UniProt 2–116 Chain W; UniProt 2–116 Chain Y; UniProt 2–116 Chain b; UniProt 2–116 Chain c; UniProt 2–116 Chain d; UniProt 2–116 Chain e; UniProt 2–116 Chain f; UniProt 2–116 Chain j; UniProt 2–116 Chain l; UniProt 2–116 Not recorded MYR MYRISTIC ACID × 24 PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 24 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.00 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.

70 other PDB entries and 103 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B6DRA0_9HIV1
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–115; UniProt 2–116 Author chain B; PDBConstruct 1–115; UniProt 2–116 Author chain C; PDBConstruct 1–115; UniProt 2–116 Author chain D; PDBConstruct 1–115; UniProt 2–116 Author chain E; PDBConstruct 1–115; UniProt 2–116 Author chain F; PDBConstruct 1–115; UniProt 2–116 Author chain H; PDBConstruct 1–115; UniProt 2–116 Author chain I; PDBConstruct 1–115; UniProt 2–116 Author chain J; PDBConstruct 1–115; UniProt 2–116 Author chain O; PDBConstruct 1–115; UniProt 2–116 Author chain P; PDBConstruct 1–115; UniProt 2–116 Author chain Q; PDBConstruct 1–115; UniProt 2–116 Author chain R; PDBConstruct 1–115; UniProt 2–116 Author chain S; PDBConstruct 1–115; UniProt 2–116 Author chain U; PDBConstruct 1–115; UniProt 2–116 Author chain W; PDBConstruct 1–115; UniProt 2–116 Author chain Y; PDBConstruct 1–115; UniProt 2–116 Author chain b; PDBConstruct 1–115; UniProt 2–116 Author chain c; PDBConstruct 1–115; UniProt 2–116 Author chain d; PDBConstruct 1–115; UniProt 2–116 Author chain e; PDBConstruct 1–115; UniProt 2–116 Author chain f; PDBConstruct 1–115; UniProt 2–116 Author chain j; PDBConstruct 1–115; UniProt 2–116 Author chain l; PDBConstruct 1–115; UniProt 2–116

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 7ovr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7ovr
Deposition date deposition_date2021-06-15
Structure title titleMature HIV-1 matrix structure
Keywords keywordsHIV-1, Gag, matrix, VIRUS; VIRUS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier66.73
Radius of gyration Rg (electron density) rg_electron67.16
Forward intensity I(0) i01058410000.00
Molecular weight molecular_weight177840.0 kDa
Excluded volume excluded_volume182120 ų
Envelope volume envelope_volume637220 ų
Hydration-shell volume shell_volume82990 ų
Envelope diameter envelope_diameter208.8
Shell Rg shell_rg62.07
Envelope Rg envelope_rg63.09
Shape Rg shape_rg67.12
Total Rg total_rg67.10
Total atoms total_atoms12528
Residues n_residues2760
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 dmax191.8
Rg (real space) rg_real66.71
Rg uncertainty (real space) rg_real_error1.75
I(0) (real space) i0_real1.0580e+09
I(0) uncertainty (real space) i0_real_error2.2330e+07
Rg (reciprocal space) rg_reciprocal66.65
I(0) (reciprocal space) i0_reciprocal1058000000.0000
Solution quality estimate total_estimate0.8461
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary83.4
Skewness Skewness skewness0.149
Kurtosis Kurtosis kurtosis-0.765
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha44400000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 1.000; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)