SAXSdb — 1l5b

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

cyanovirin-N

Nostoc ellipsosporum

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	SODIUM ION × 1 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CVN_NOSEL
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–101； UniProt 1–101 Author chain B； PDBConstruct 1–101； UniProt 1–101

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	1l5b
Deposition date deposition_date	2002-03-06
Structure title title	DOMAIN-SWAPPED CYANOVIRIN-N DIMER
Keywords keywords	CYANOVIRIN-N, HIV-INACTIVATING, DOMAIN-SWAPPING, GP120, ANTIVIRAL PROTEIN; ANTIVIRAL 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.

1l5b__assembly_1__model_1

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

Download this curve (.dat)

1l5b__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1l5b__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	18.96 Å
Rg (electron density)	17.74 Å
Total Rg	18.61 Å
Atom count	1554
Residues	202
Excluded volume	27241 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1l5b__assembly_1__model_1`	dimeric （2）	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 (4)

Entity 1 Entity 1 polymer

Description description	cyanovirin-N
Molecular weight formula_weight	11022.1 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	1749

LGKFSQTCYNSAIQGSVLTSTCERTNGGYNTSSIDLNSVIENVDGSLKWQPSNFIETCRNTQLAGSSELAAECKTRAQQFVSTKINLDDHIANIDGTLKYE

Source Source

Source organism organism	Nostoc ellipsosporum
NCBI taxonomy ID ncbi_taxonomy_id	45916
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID
Molecular weight formula_weight	207.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	195

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1l5ba_
Class class	b — All beta proteins
Fold Fold fold	b.89 — Cyanovirin-N
Superfamily Superfamily superfamily	b.89.1 — Cyanovirin-N
Family Family family	b.89.1.1 — Cyanovirin-N

Domain ID domain_id	d1l5bb_
Class class	b — All beta proteins
Fold Fold fold	b.89 — Cyanovirin-N
Superfamily Superfamily superfamily	b.89.1 — Cyanovirin-N
Family Family family	b.89.1.1 — Cyanovirin-N

CATH v4.4 (2 domains)

Domain ID domain_id	1l5bA00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	60 — HIV-inactivating Protein, Cyanovirin-n
Homologous superfamily homologous superfamily	10 — Cyanovirin-N

Domain ID domain_id	1l5bB00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	60 — HIV-inactivating Protein, Cyanovirin-n
Homologous superfamily homologous superfamily	10 — Cyanovirin-N

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Unit-cell length a length_a	61.966 Å
Unit-cell length b length_b	61.966 Å
Unit-cell length c length_c	148.400 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	16

Space group space_group	P 41 21 2
Space-group number int_tables_number	92
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	19.900 Å
R factor r_factor	—
R_work r_work	0.2470
R_free r_free	0.2580

DOMAIN-SWAPPED CYANOVIRIN-N DIMER

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

cyanovirin-N

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

1l5b__assembly_1__model_1

1l5b__assembly_1__model_1 | I(q)

1l5b__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

DOMAIN-SWAPPED CYANOVIRIN-N DIMER

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

cyanovirin-N

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

1l5b__assembly_1__model_1

1l5b__assembly_1__model_1 | I(q)

1l5b__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)