9u51

Cryo-EM structure of Mycobacterium tuberculosis MmpL5 in complex with AcpM

Method: ELECTRON MICROSCOPY Dmax: 122.9 Å Quality: GOOD

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

Siderophore exporter MmpL5

Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

UniProt P9WJV1

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–964 Not recorded Meromycolate extension acyl carrier protein × 1 (A0R0B3) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.05 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 MMPL5_MYCTU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–964; UniProt 1–964

Meromycolate extension acyl carrier protein

Mycolicibacterium smegmatis MC2 155

UniProt A0R0B3

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–99 Non-standard monomer:Yes (specific site not provided by mmCIF) Siderophore exporter MmpL5 × 1 (P9WJV1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.05 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.

18 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACPM_MYCS2
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–99; UniProt 1–99

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 9u51

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9u51
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9u51
Deposition date deposition_date2025-03-20
Structure title titleCryo-EM structure of Mycobacterium tuberculosis MmpL5 in complex with AcpM
Keywords keywordsMycobacterium tuberculosis efflux pump MmpL5 in complex with meromycolate extension acyl carrier protein AcpM, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.84
Radius of gyration Rg (electron density) rg_electron35.50
Forward intensity I(0) i0107461000.00
Molecular weight molecular_weight86974.0 kDa
Excluded volume excluded_volume110720 ų
Envelope volume envelope_volume146300 ų
Hydration-shell volume shell_volume37337 ų
Envelope diameter envelope_diameter129.8
Shell Rg shell_rg38.45
Envelope Rg envelope_rg35.71
Shape Rg shape_rg35.55
Total Rg total_rg35.55
Total atoms total_atoms6118
Residues n_residues809
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 dmax122.9
Rg (real space) rg_real36.27
Rg uncertainty (real space) rg_real_error1.25
I(0) (real space) i0_real1.0750e+08
I(0) uncertainty (real space) i0_real_error1.9350e+06
Rg (reciprocal space) rg_reciprocal36.00
I(0) (reciprocal space) i0_reciprocal107400000.0000
Solution quality estimate total_estimate0.7844
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.7
Skewness Skewness skewness0.601
Kurtosis Kurtosis kurtosis-0.285
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha33480000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.669; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.668; Smooth: 0.518

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)