9mw0

Bipartite complex of MmpL5-AcpM from Mycolicibacterium smegmatis

Method: ELECTRON MICROSCOPY Dmax: 153.8 Å Quality: GOOD

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

MmpL5 protein

Mycolicibacterium smegmatis

UniProt A0QS80

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain D; UniProt 1–967 Chain E; UniProt 1–967 Chain F; UniProt 1–967 Not recorded Meromycolate extension acyl carrier protein × 3 (A0R0B3) PNS 4'-PHOSPHOPANTETHEINE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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 A0QS80_MYCS2
Isoform
PDB entities 1
Chains and sequence ranges Author chain D; PDBConstruct 1–967; UniProt 1–967 Author chain E; PDBConstruct 1–967; UniProt 1–967 Author chain F; PDBConstruct 1–967; UniProt 1–967

Meromycolate extension acyl carrier protein

Mycolicibacterium smegmatis

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain G; UniProt 1–99 Chain H; UniProt 1–99 Chain I; UniProt 1–99 Not recorded MmpL5 protein × 3 (A0QS80) PNS 4'-PHOSPHOPANTETHEINE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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 G; PDBConstruct 1–99; UniProt 1–99 Author chain H; PDBConstruct 1–99; UniProt 1–99 Author chain I; 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 9mw0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9mw0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9mw0
Deposition date deposition_date2025-01-16
Structure title titleBipartite complex of MmpL5-AcpM from Mycolicibacterium smegmatis
Keywords keywordsMycolicibacterium smegmatis, MmpL5, AcpM, membrane protein, bipartite complex; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.85
Radius of gyration Rg (electron density) rg_electron46.93
Forward intensity I(0) i01051020000.00
Molecular weight molecular_weight279530.0 kDa
Excluded volume excluded_volume353950 ų
Envelope volume envelope_volume492570 ų
Hydration-shell volume shell_volume84532 ų
Envelope diameter envelope_diameter163.1
Shell Rg shell_rg54.17
Envelope Rg envelope_rg45.99
Shape Rg shape_rg46.96
Total Rg total_rg47.08
Total atoms total_atoms19668
Residues n_residues2589
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 dmax153.8
Rg (real space) rg_real47.55
Rg uncertainty (real space) rg_real_error1.20
I(0) (real space) i0_real1.0510e+09
I(0) uncertainty (real space) i0_real_error2.0110e+07
Rg (reciprocal space) rg_reciprocal47.85
I(0) (reciprocal space) i0_reciprocal1051000000.0000
Solution quality estimate total_estimate0.8818
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary65.2
Skewness Skewness skewness0.093
Kurtosis Kurtosis kurtosis-0.391
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha96850000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.855; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.918

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)