3cyo

Structure of a longer thermalstable core domain of HIV-1 GP41 containing the enfuvirtide resistance mutation N43D and complementary mutation E137K

Method: X-RAY DIFFRACTION

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

Transmembrane protein

Human immunodeficiency virus type 1

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 3	water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ENV_HV1LW
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–44； UniProt 536–579 Author chain A； PDBConstruct 51–86； UniProt 628–663

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3cyo
Deposition date deposition_date	2008-04-25
Structure title title	Structure of a longer thermalstable core domain of HIV-1 GP41 containing the enfuvirtide resistance mutation N43D and complementary mutation E137K
Keywords keywords	;HIV-1 ENVELOPE GLYCOPROTEIN, 6-HELIX BUNDLE, GP41, N43D, E137K, AIDS, APOPTOSIS, COILED COIL, ENVELOPE PROTEIN, FUSION PROTEIN, HOST-VIRUS INTERACTION, MEMBRANE, TRANSMEMBRANE, VIRION, VIRAL PROTEIN, Cleavage on pair of basic residues, Lipoprotein, Palmitate, Viral immunoevasion ;; VIRAL PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

3cyo__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

3cyo__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3cyo__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	19.30 Å
Rg (electron density)	18.60 Å
Total Rg	19.50 Å
Atom count	1815
Residues	219
Excluded volume	32103 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3cyo__assembly_1__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (2)

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d3cyoa_
Class class	h — Coiled coil proteins
Fold Fold fold	h.3 — Stalk segment of viral fusion proteins
Superfamily Superfamily superfamily	h.3.2 — Virus ectodomain
Family Family family	h.3.2.1 — Virus ectodomain

CATH v4.4 (1 domains)

Domain ID domain_id	3cyoA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	210 —

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Unit-cell length a length_a	59.290 Å
Unit-cell length b length_b	59.290 Å
Unit-cell length c length_c	59.290 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	P 21 3
Space-group number int_tables_number	198
Crystal system crystal_system	—

Resolution resolution	2.100 Å
Low-resolution limit resolution_low	50.000 Å
R factor r_factor	0.2420
R_work r_work	0.2420
R_free r_free	0.3320

Description description	Transmembrane protein
Molecular weight formula_weight	9975.2 kDa
Mutation mutation	N554D,E648K
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	632

Structure of a longer thermalstable core domain of HIV-1 GP41 containing the enfuvirtide resistance mutation N43D and complementary mutation E137K

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

Transmembrane protein

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

3cyo__assembly_1__model_1

3cyo__assembly_1__model_1 | I(q)

3cyo__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)

Source organism organism	Human immunodeficiency virus type 1
Host organism host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	27

Structure of a longer thermalstable core domain of HIV-1 GP41 containing the enfuvirtide resistance mutation N43D and complementary mutation E137K

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

Transmembrane protein

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

3cyo__assembly_1__model_1

3cyo__assembly_1__model_1 | I(q)

3cyo__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)