1ce0

TRIMERIZATION SPECIFICITY IN HIV-1 GP41: ANALYSIS WITH A GCN4 LEUCINE ZIPPER MODEL

Method: X-RAY DIFFRACTION Dmax: 59.6 Å Quality: GOOD

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

PROTEIN (LEUCINE ZIPPER MODEL H38-P1)

Human immunodeficiency virus 1

UniProt Q7SIH0

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–37 Chain B; UniProt 1–37 Chain C; UniProt 1–37 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;pH 7.5 Resolution 2.40 Å R-free 0.294

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q7SIH0_9HIV1
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–37; UniProt 1–37 Author chain B; PDBConstruct 1–37; UniProt 1–37 Author chain C; PDBConstruct 1–37; UniProt 1–37

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 1ce0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ce0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1ce0
Deposition date deposition_date1999-03-12
Structure title titleTRIMERIZATION SPECIFICITY IN HIV-1 GP41: ANALYSIS WITH A GCN4 LEUCINE ZIPPER MODEL
Keywords keywordsHIV-1 ENVELOPE PROTEIN, GP41, PROTEIN OLIGOMERIZATION, COILED COIL, LEUCINE ZIPPER; HIV-1 ENVELOPE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.69
Radius of gyration Rg (electron density) rg_electron16.39
Forward intensity I(0) i02952000.00
Molecular weight molecular_weight12669.0 kDa
Excluded volume excluded_volume16182 ų
Envelope volume envelope_volume18494 ų
Hydration-shell volume shell_volume10631 ų
Envelope diameter envelope_diameter55.0
Shell Rg shell_rg20.19
Envelope Rg envelope_rg16.72
Shape Rg shape_rg16.33
Total Rg total_rg17.30
Total atoms total_atoms892
Residues n_residues106
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 dmax59.6
Rg (real space) rg_real16.81
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real2.9520e+06
I(0) uncertainty (real space) i0_real_error3.5600e+04
Rg (reciprocal space) rg_reciprocal16.80
I(0) (reciprocal space) i0_reciprocal2952000.0000
Solution quality estimate total_estimate0.7820
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.8
Skewness Skewness skewness0.532
Kurtosis Kurtosis kurtosis-0.228
Angular range angular_range— – 0.4750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1216000.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.473; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.752; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1ce0a_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.3 — Leucine zipper domain
Family Family familyh.1.3.1 — Leucine zipper domain
Domain ID domain_idd1ce0b_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.3 — Leucine zipper domain
Family Family familyh.1.3.1 — Leucine zipper domain
Domain ID domain_idd1ce0c_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.3 — Leucine zipper domain
Family Family familyh.1.3.1 — Leucine zipper domain

8. Citations (3)

9. Files and Curves (10)