9fqt

Cryo-EM structure of MmCAT1 bound with FrMLV-RBD in the apo inward-open state

Method: ELECTRON MICROSCOPY Dmax: 109.7 Å Quality: GOOD

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

High affinity cationic amino acid transporter 1,Green fluorescent protein

Mus musculus

UniProt P42212

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 其他Polymer 3 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–238 Not recorded Surface protein × 1 (P03390) ;alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 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

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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 623–859; UniProt 2–238

High affinity cationic amino acid transporter 1,Green fluorescent protein

Mus musculus

UniProt Q09143

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 其他Polymer 3 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 13–622 Not recorded Surface protein × 1 (P03390) ;alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 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

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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CTR1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–610; UniProt 13–622

Surface protein

Murine leukemia virus

UniProt P03390

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 其他Polymer 3 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 35–270 Not recorded High affinity cationic amino acid transporter 1,Green fluorescent protein × 1 (Q09143,P42212) ;alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 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

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.

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 2
Chains and sequence ranges Author chain B; PDBConstruct 32–267; UniProt 35–270

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.

SAXS scattering curve SAXS Profile

SAXS profile for 9fqt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9fqt
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9fqt
Deposition date deposition_date2024-06-17
Structure title titleCryo-EM structure of MmCAT1 bound with FrMLV-RBD in the apo inward-open state
Keywords keywordsMmCAT1, FrMLV-RBD, SLC, viral tropism, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier32.27
Radius of gyration Rg (electron density) rg_electron31.87
Forward intensity I(0) i0100468000.00
Molecular weight molecular_weight84121.0 kDa
Excluded volume excluded_volume107060 ų
Envelope volume envelope_volume132630 ų
Hydration-shell volume shell_volume35768 ų
Envelope diameter envelope_diameter116.1
Shell Rg shell_rg37.36
Envelope Rg envelope_rg32.10
Shape Rg shape_rg31.92
Total Rg total_rg32.19
Total atoms total_atoms11733
Residues n_residues760
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 dmax109.7
Rg (real space) rg_real32.46
Rg uncertainty (real space) rg_real_error0.92
I(0) (real space) i0_real1.0050e+08
I(0) uncertainty (real space) i0_real_error1.6190e+06
Rg (reciprocal space) rg_reciprocal32.38
I(0) (reciprocal space) i0_reciprocal100500000.0000
Solution quality estimate total_estimate0.8646
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.3
Skewness Skewness skewness0.451
Kurtosis Kurtosis kurtosis-0.352
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14530000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.822; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.906; Smooth: 0.863

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)