1gzl

Crystal structure of C14linkmid/IQN17: a cross-linked inhibitor of HIV-1 entry bound to the gp41 hydrophobic pocket

Method: X-RAY DIFFRACTION Dmax: 125.7 Å Quality: SUSPICIOUS

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

FUSION PROTEIN BETWEEN THE HYDROPHOBIC POCKET OF HIV GP41 AND GENERAL CONTROL PROTEIN GCN4-PIQI

OrganismNot specified

UniProt P03069

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 249–276 Fragment:GP41 HYDROPHOBIC POCKET, RESIDUES 565-581, GCN4, RESIDUES 249-276 Non-standard monomer:Yes (specific site not provided by mmCIF) ENVELOPE GLYCOPROTEIN GP41 × 3 (P04578) CL CHLORIDE ION × 3 N2P PENTANE-1,5-DIAMINE × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.6;16% ISOPROPANOL, 0.1 M TRIS, PH 8.6, 1 M (NH4)2SO4 Resolution 1.80 Å R-free 0.243
2 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 249–276 Fragment:GP41 HYDROPHOBIC POCKET, RESIDUES 565-581, GCN4, RESIDUES 249-276 Non-standard monomer:Yes (specific site not provided by mmCIF) ENVELOPE GLYCOPROTEIN GP41 × 3 (P04578) CL CHLORIDE ION × 3 N2P PENTANE-1,5-DIAMINE × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.6;16% ISOPROPANOL, 0.1 M TRIS, PH 8.6, 1 M (NH4)2SO4 Resolution 1.80 Å R-free 0.243

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.

162 other PDB entries and 199 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCN4_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–29; UniProt 249–276 Author chain B; PDBConstruct 2–29; UniProt 249–276

FUSION PROTEIN BETWEEN THE HYDROPHOBIC POCKET OF HIV GP41 AND GENERAL CONTROL PROTEIN GCN4-PIQI

OrganismNot specified

UniProt P04578

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 565–581 Chain C; UniProt 628–639 Fragment:GP41 HYDROPHOBIC POCKET, RESIDUES 565-581, GCN4, RESIDUES 249-276 Non-standard monomer:Yes (specific site not provided by mmCIF) Fragment:RESIDUES 628-639 Mutation:YES CL CHLORIDE ION × 3 N2P PENTANE-1,5-DIAMINE × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.6;16% ISOPROPANOL, 0.1 M TRIS, PH 8.6, 1 M (NH4)2SO4 Resolution 1.80 Å R-free 0.243
2 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 565–581 Chain D; UniProt 628–639 Fragment:GP41 HYDROPHOBIC POCKET, RESIDUES 565-581, GCN4, RESIDUES 249-276 Non-standard monomer:Yes (specific site not provided by mmCIF) Fragment:RESIDUES 628-639 Mutation:YES CL CHLORIDE ION × 3 N2P PENTANE-1,5-DIAMINE × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.6;16% ISOPROPANOL, 0.1 M TRIS, PH 8.6, 1 M (NH4)2SO4 Resolution 1.80 Å R-free 0.243

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.

38 other PDB entries and 48 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ENV_HV1H2
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 30–46; UniProt 565–581 Author chain B; PDBConstruct 30–46; UniProt 565–581 Author chain C; PDBConstruct 1–12; UniProt 628–639 Author chain D; PDBConstruct 1–12; UniProt 628–639

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 1gzl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1gzl
Deposition date deposition_date2002-05-23
Structure title titleCrystal structure of C14linkmid/IQN17: a cross-linked inhibitor of HIV-1 entry bound to the gp41 hydrophobic pocket
Keywords keywordsGLYCOPROTEIN, HIV ENTRY, INHIBITOR, CROSS-LINK, GP41, COILED COIL; GLYCOPROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier35.66
Radius of gyration Rg (electron density) rg_electron36.14
Forward intensity I(0) i03332440.00
Molecular weight molecular_weight14500.0 kDa
Excluded volume excluded_volume18475 ų
Envelope volume envelope_volume31073 ų
Hydration-shell volume shell_volume8819 ų
Envelope diameter envelope_diameter131.2
Shell Rg shell_rg33.09
Envelope Rg envelope_rg36.23
Shape Rg shape_rg35.94
Total Rg total_rg36.46
Total atoms total_atoms1018
Residues n_residues114
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 dmax125.7
Rg (real space) rg_real36.52
Rg uncertainty (real space) rg_real_error1.87
I(0) (real space) i0_real3.3320e+06
I(0) uncertainty (real space) i0_real_error6.8830e+04
Rg (reciprocal space) rg_reciprocal35.99
I(0) (reciprocal space) i0_reciprocal3331000.0000
Solution quality estimate total_estimate0.3881
Solution quality rating solution_quality SUSPICIOUS a SUSPICIOUS solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary11.4
Skewness Skewness skewness0.526
Kurtosis Kurtosis kurtosis-0.444
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha155600.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.047; Stabil: 1.000; Sysdev: 0.101; Positv: 1.000; Valcen: 0.085; Smooth: 0.513

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1gzl.1
Class classh — Coiled coil proteins
Fold Fold foldh.3 — Stalk segment of viral fusion proteins
Superfamily Superfamily superfamilyh.3.2 — Virus ectodomain
Family Family familyh.3.2.1 — Virus ectodomain
Domain ID domain_idd1gzl.2
Class classh — Coiled coil proteins
Fold Fold foldh.3 — Stalk segment of viral fusion proteins
Superfamily Superfamily superfamilyh.3.2 — Virus ectodomain
Family Family familyh.3.2.1 — Virus ectodomain

CATH v4.4 (2 domains)

Domain ID domain_id1gzlA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily170
Domain ID domain_id1gzlB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily170

8. Citations (1)

9. Files and Curves (10)