SAXSdb — 1aol

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

GP70

Friend murine leukemia virus

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 43–270	Fragment：RECEPTOR-BINDING DOMAIN	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；PROTEIN WAS CRYSTALLIZED FROM 150 MM ZINC ACETATE, 100 MM SODIUM CACODYLATE, PH 6.5, 19% PEG 8000	Resolution 2.00 Å R-free 0.264

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.

Other PDB	Difference from Current Entry 1AOL	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9FQT Cryo-EM structure of MmCAT1 bound with FrMLV-RBD in the apo inward-open state Deposited 2024-06-17	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 35–270（236 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 Y01 CHOLESTEROL HEMISUCCINATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
9FQU Cryo-EM structure of MmCAT1 bound with FrMLV-RBD in the arginine-bound inward-occluded state Deposited 2024-06-17	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 35–270（236 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 Y01 CHOLESTEROL HEMISUCCINATE × 2 ARG ARGININE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.79 Å
9FQV Cryo-EM structure of MmCAT1 bound with FrMLV-RBD in the lysine-bound inward-occluded state Deposited 2024-06-17	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 35–270（236 aa）	Not recorded	LYS LYSINE × 1 Y01 CHOLESTEROL HEMISUCCINATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.95 Å
9FQW Cryo-EM structure of MmCAT1 bound with FrMLV-RBD in the ornithine-bound inward-occluded state Deposited 2024-06-17	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 35–270（236 aa）	Not recorded	Y01 CHOLESTEROL HEMISUCCINATE × 2 ORN L-ornithine × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.01 Å
9UAT The structure of mCAT1 in complex with its substrate ornithine and the RBD of FrMLV. Deposited 2025-04-01	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 36–264（229 aa）	Not recorded	ORN L-ornithine × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.65 Å

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ENV_MLVF5
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–228； UniProt 43–270

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	1aol
Deposition date deposition_date	1997-07-08
Structure title title	FRIEND MURINE LEUKEMIA VIRUS RECEPTOR-BINDING DOMAIN
Keywords keywords	COAT PROTEIN, VIRAL GLYCOPROTEIN, RETROVIRUS, Viral protein; VIRAL PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	19.40 Å
Radius of gyration Rg (electron density) rg_electron	18.34 Å
Forward intensity I(0) i0	13091900.00
Molecular weight molecular_weight	25947.0 kDa
Excluded volume excluded_volume	31873 Å³
Envelope volume envelope_volume	36203 Å³
Hydration-shell volume shell_volume	17022 Å³
Envelope diameter envelope_diameter	67.0 Å
Shell Rg shell_rg	24.14 Å
Envelope Rg envelope_rg	18.91 Å
Shape Rg shape_rg	18.26 Å
Total Rg total_rg	19.39 Å
Total atoms total_atoms	1816
Residues n_residues	228
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	67.4 Å
Rg (real space) rg_real	19.39 Å
Rg uncertainty (real space) rg_real_error	0.53 Å
I(0) (real space) i0_real	1.3090e+07
I(0) uncertainty (real space) i0_real_error	1.8990e+05
Rg (reciprocal space) rg_reciprocal	19.39 Å
I(0) (reciprocal space) i0_reciprocal	13090000.0000
Solution quality estimate total_estimate	0.8595
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	22.8 Å
Skewness Skewness skewness	0.357
Kurtosis Kurtosis kurtosis	-0.263
Angular range angular_range	— – 0.4100 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2173000.0000
Real-space data points n_real_points	72
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.776; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.935; Smooth: 0.907

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	GP70
Molecular weight formula_weight	25397.4 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2007

QVYNITWEVTNGDRETVWAISGNHPLWTWWPVLTPDLCMLALSGPPHWGLEYQAPYSSPPGPPCCSGSSGSSAGCSRDCDEPLTSLTPRCNTAWNRLKLDQVTHKSSEGFYVCPGSHRPREAKSCGGPDSFYCASWGCETTGRVYWKPSSSWDYITVDNNLTTSQAVQVCKDNKWCNPLAIQFTNAGKQVTSWTTGHYWGLRLYVSGRDPGLTFGIRLRYQNLGPRVP

来源 Source

来源生物 organism	Friend murine leukemia virus
NCBI Class编号 ncbi_taxonomy_id	11795
宿主生物 host_organism	Trichoplusia ni

Entity 2 Entity 2 non-polymer

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	221.2 kDa
Source method src_method	man
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	191

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1aola_
Class class	b — All beta proteins
Fold Fold fold	b.20 — ENV polyprotein, receptor-binding domain
Superfamily Superfamily superfamily	b.20.1 — ENV polyprotein, receptor-binding domain
Family Family family	b.20.1.1 — ENV polyprotein, receptor-binding domain

CATH v4.4 (1 domains)

Domain ID domain_id	1aolA00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	310 — Viral Glycoprotein Gp70
Homologous superfamily homologous superfamily	10 — ENV polyprotein, receptor-binding domain

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8. Citations (1)

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Unit-cell length a length_a	55.300 Å
Unit-cell length b length_b	68.400 Å
Unit-cell length c length_c	80.400 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	4

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.2230
R_work r_work	0.2230
R_free r_free	0.2640

fit	/app/data/saxs_computation/ao/1aol/1aol.fit
pddf	/app/data/pr_computation/ao/1aol/1aol.pr.out
profile	/app/data/saxs_computation/ao/1aol/1aol.dat

FRIEND MURINE LEUKEMIA VIRUS RECEPTOR-BINDING DOMAIN

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

GP70

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction