SAXSdb — 4v5t

▼

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

COAT PROTEIN

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 60	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	POL2_GFLV
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain AA； PDBConstruct 1–504； UniProt 606–1109 Author chain AB； PDBConstruct 1–504； UniProt 606–1109 Author chain AC； PDBConstruct 1–504； UniProt 606–1109 Author chain AD； PDBConstruct 1–504； UniProt 606–1109 Author chain AE； PDBConstruct 1–504； UniProt 606–1109 Author chain AF； PDBConstruct 1–504； UniProt 606–1109 Author chain AG； PDBConstruct 1–504； UniProt 606–1109 Author chain AH； PDBConstruct 1–504； UniProt 606–1109 Author chain AI； PDBConstruct 1–504； UniProt 606–1109 Author chain AJ； PDBConstruct 1–504； UniProt 606–1109 Author chain AK； PDBConstruct 1–504； UniProt 606–1109 Author chain AL； PDBConstruct 1–504； UniProt 606–1109 Author chain AM； PDBConstruct 1–504； UniProt 606–1109 Author chain AN； PDBConstruct 1–504； UniProt 606–1109 Author chain AO； PDBConstruct 1–504； UniProt 606–1109 Author chain AP； PDBConstruct 1–504； UniProt 606–1109 Author chain AQ； PDBConstruct 1–504； UniProt 606–1109 Author chain AR； PDBConstruct 1–504； UniProt 606–1109 Author chain AS； PDBConstruct 1–504； UniProt 606–1109 Author chain AT； PDBConstruct 1–504； UniProt 606–1109 Author chain BA； PDBConstruct 1–504； UniProt 606–1109 Author chain BB； PDBConstruct 1–504； UniProt 606–1109 Author chain BC； PDBConstruct 1–504； UniProt 606–1109 Author chain BD； PDBConstruct 1–504； UniProt 606–1109 Author chain BE； PDBConstruct 1–504； UniProt 606–1109 Author chain BF； PDBConstruct 1–504； UniProt 606–1109 Author chain BG； PDBConstruct 1–504； UniProt 606–1109 Author chain BH； PDBConstruct 1–504； UniProt 606–1109 Author chain BI； PDBConstruct 1–504； UniProt 606–1109 Author chain BJ； PDBConstruct 1–504； UniProt 606–1109 Author chain BK； PDBConstruct 1–504； UniProt 606–1109 Author chain BL； PDBConstruct 1–504； UniProt 606–1109 Author chain BM； PDBConstruct 1–504； UniProt 606–1109 Author chain BN； PDBConstruct 1–504； UniProt 606–1109 Author chain BO； PDBConstruct 1–504； UniProt 606–1109 Author chain BP； PDBConstruct 1–504； UniProt 606–1109 Author chain BQ； PDBConstruct 1–504； UniProt 606–1109 Author chain BR； PDBConstruct 1–504； UniProt 606–1109 Author chain BS； PDBConstruct 1–504； UniProt 606–1109 Author chain BT； PDBConstruct 1–504； UniProt 606–1109 Author chain CA； PDBConstruct 1–504； UniProt 606–1109 Author chain CB； PDBConstruct 1–504； UniProt 606–1109 Author chain CC； PDBConstruct 1–504； UniProt 606–1109 Author chain CD； PDBConstruct 1–504； UniProt 606–1109 Author chain CE； PDBConstruct 1–504； UniProt 606–1109 Author chain CF； PDBConstruct 1–504； UniProt 606–1109 Author chain CG； PDBConstruct 1–504； UniProt 606–1109 Author chain CH； PDBConstruct 1–504； UniProt 606–1109 Author chain CI； PDBConstruct 1–504； UniProt 606–1109 Author chain CJ； PDBConstruct 1–504； UniProt 606–1109 Author chain CK； PDBConstruct 1–504； UniProt 606–1109 Author chain CL； PDBConstruct 1–504； UniProt 606–1109 Author chain CM； PDBConstruct 1–504； UniProt 606–1109 Author chain CN； PDBConstruct 1–504； UniProt 606–1109 Author chain CO； PDBConstruct 1–504； UniProt 606–1109 Author chain CP； PDBConstruct 1–504； UniProt 606–1109 Author chain CQ； PDBConstruct 1–504； UniProt 606–1109 Author chain CR； PDBConstruct 1–504； UniProt 606–1109 Author chain CS； PDBConstruct 1–504； UniProt 606–1109 Author chain CT； PDBConstruct 1–504； UniProt 606–1109

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	4v5t
Deposition date deposition_date	2011-02-01
Structure title title	X-ray structure of the Grapevine Fanleaf virus
Keywords keywords	VIRUS, FANLEAF DISEASE; VIRUS
Experimental Method method	X-RAY DIFFRACTION

▼

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.

4v5t__assembly_1__model_1

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

Download this curve (.dat)

4v5t__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4v5t__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	0.00 Å
Rg (electron density)	129.30 Å
Total Rg	129.50 Å
Atom count	237060
Residues	30240
Excluded volume	4251000 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4v5t__assembly_1__model_1`	60-meric （60）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (1)

▶

Unit-cell length a length_a	279.400 Å
Unit-cell length b length_b	279.600 Å
Unit-cell length c length_c	293.300 Å
Unit-cell angle α angle_alpha	102.40 °
Unit-cell angle β angle_beta	116.40 °
Unit-cell angle γ angle_gamma	108.20 °
Molecules per unit cell Z z_pdb	60

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	3.000 Å
Low-resolution limit resolution_low	135.426 Å
R factor r_factor	0.1911
R_work r_work	0.1902
R_free r_free	0.2073

Description description	COAT PROTEIN
Molecular weight formula_weight	56073.1 kDa
Source method src_method	nat
Copy count entity_count	60

Polymer type type	polypeptide(L)
Chain IDs strand_id	;AA,AB,AC,AD,AE,AF,AG,AH,AI,AJ,AK,AL,AM,AN,AO,AP,AQ,AR,AS,AT,BA,BB,BC,BD,BE,BF,BG,BH,BI,BJ,BK,BL,BM,BN,BO,BP,BQ,BR,BS,BT,CA,CB,CC,CD,CE,CF,CG,CH,CI,CJ,CK,CL,CM,CN,CO,CP,CQ,CR,CS,CT ;
Atom count atom_count	237060

X-ray structure of the Grapevine Fanleaf virus

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

COAT 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

4v5t__assembly_1__model_1

4v5t__assembly_1__model_1 | I(q)

4v5t__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

7. Citations (2)

X-ray structure of the Grapevine Fanleaf virus

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

COAT 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

4v5t__assembly_1__model_1

4v5t__assembly_1__model_1 | I(q)

4v5t__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

7. Citations (2)