2nxz

HIV-1 gp120 Envelope Glycoprotein (T257S, S334A, S375W) Complexed with CD4 and Antibody 17b

Method: X-RAY DIFFRACTION Dmax: 135.7 Å Quality: GOOD

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

ENVELOPE GLYCOPROTEIN GP120

Human immunodeficiency virus 1

UniProt Q8QDX5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 157–468 Fragment:CORE Mutation:T257S, S334A, S375W T-cell surface glycoprotein CD4 × 1 (P01730) ANTIBODY 17B, LIGHT CHAIN × 1 (Q6P5S8) ANTIBODY 17B, HEAVY CHAIN × 1 (Q6PJA4) beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 13 EDO 1,2-ETHANEDIOL × 3 HEZ HEXANE-1,6-DIOL × 1 IPA ISOPROPYL ALCOHOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;298 K;7.5% PEG 4000, 8.5% MPD, 100 mM Na Citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.04 Å R-free 0.244

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8QDX5_9HIV1
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–317; UniProt 157–468

T-cell surface glycoprotein CD4

Homo sapiens

UniProt P01730

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 26–208 Fragment:D1D2, N-TERMINAL TWO DOMAIN FRAGMENT ENVELOPE GLYCOPROTEIN GP120 × 1 (Q8QDX5) ANTIBODY 17B, LIGHT CHAIN × 1 (Q6P5S8) ANTIBODY 17B, HEAVY CHAIN × 1 (Q6PJA4) beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 13 EDO 1,2-ETHANEDIOL × 3 HEZ HEXANE-1,6-DIOL × 1 IPA ISOPROPYL ALCOHOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;298 K;7.5% PEG 4000, 8.5% MPD, 100 mM Na Citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.04 Å R-free 0.244

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.

78 other PDB entries and 99 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CD4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–184; UniProt 26–208

ANTIBODY 17B, LIGHT CHAIN

Homo sapiens

UniProt Q6P5S8

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 22–234 Fragment:ANTIGEN-BINDING FRAGMENT, FAB ENVELOPE GLYCOPROTEIN GP120 × 1 (Q8QDX5) T-cell surface glycoprotein CD4 × 1 (P01730) ANTIBODY 17B, HEAVY CHAIN × 1 (Q6PJA4) beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 13 EDO 1,2-ETHANEDIOL × 3 HEZ HEXANE-1,6-DIOL × 1 IPA ISOPROPYL ALCOHOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;298 K;7.5% PEG 4000, 8.5% MPD, 100 mM Na Citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.04 Å R-free 0.244

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.

16 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q6P5S8_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 2–214; UniProt 22–234

ANTIBODY 17B, HEAVY CHAIN

Homo sapiens

UniProt Q6PJA4

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 20–241 Fragment:ANTIGEN-BINDING FRAGMENT, FAB ENVELOPE GLYCOPROTEIN GP120 × 1 (Q8QDX5) T-cell surface glycoprotein CD4 × 1 (P01730) ANTIBODY 17B, LIGHT CHAIN × 1 (Q6P5S8) beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 13 EDO 1,2-ETHANEDIOL × 3 HEZ HEXANE-1,6-DIOL × 1 IPA ISOPROPYL ALCOHOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;298 K;7.5% PEG 4000, 8.5% MPD, 100 mM Na Citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.04 Å R-free 0.244

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.

6 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q6PJA4_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–229; UniProt 20–241

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 2nxz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2nxz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2nxz
Deposition date deposition_date2006-11-20
Structure title titleHIV-1 gp120 Envelope Glycoprotein (T257S, S334A, S375W) Complexed with CD4 and Antibody 17b
Keywords keywordsHIV, gp120, antibody, CD4, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX; VIRAL PROTEIN/IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.04
Radius of gyration Rg (electron density) rg_electron39.23
Forward intensity I(0) i0170589000.00
Molecular weight molecular_weight104440.0 kDa
Excluded volume excluded_volume130310 ų
Envelope volume envelope_volume179330 ų
Hydration-shell volume shell_volume40666 ų
Envelope diameter envelope_diameter142.3
Shell Rg shell_rg41.65
Envelope Rg envelope_rg39.02
Shape Rg shape_rg39.21
Total Rg total_rg39.45
Total atoms total_atoms7334
Residues n_residues923
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 dmax135.7
Rg (real space) rg_real39.34
Rg uncertainty (real space) rg_real_error1.72
I(0) (real space) i0_real1.7060e+08
I(0) uncertainty (real space) i0_real_error2.6710e+06
Rg (reciprocal space) rg_reciprocal39.17
I(0) (reciprocal space) i0_reciprocal170600000.0000
Solution quality estimate total_estimate0.8492
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.9
Skewness Skewness skewness0.402
Kurtosis Kurtosis kurtosis-0.566
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16390000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.790; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.752; Smooth: 0.913

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

7. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (7 domains)

Domain ID domain_idd2nxza1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.172 — gp120 core
Superfamily Superfamily superfamilyd.172.1 — gp120 core
Family Family familyd.172.1.1 — gp120 core
Domain ID domain_idd2nxzb1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd2nxzb2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.3 — C2 set domains
Domain ID domain_idd2nxzc1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd2nxzc2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)
Domain ID domain_idd2nxzd1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd2nxzd2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)

CATH v4.4 (7 domains)

Domain ID domain_id2nxzA00
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology40 — HIV Envelope Protein Gp120; Chain G
Homologous superfamily homologous superfamily20 — Human immunodeficiency virus 1, Gp160, envelope glycoprotein
Domain ID domain_id2nxzB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2nxzB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2nxzC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2nxzC02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2nxzD01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2nxzD02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)