9s2u

1:1 complex of M.tuberculosis MmpL5 and M.smegmatis AcpM

Method: ELECTRON MICROSCOPY Dmax: 117.2 Å Quality: GOOD

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

Siderophore exporter MmpL5,Green fluorescent protein

Aequorea victoria

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 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 2–238 Not recorded Meromycolate extension acyl carrier protein × 1 (A0R0B3) ELECTRON MICROSCOPY cryo-EM buffer:pH 8;50 mM HEPES pH8.0, 150 mM NaCl, 0.004% LMNG, 50 uM Bedaquiline cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 D; PDBConstruct 782–1018; UniProt 2–238

Siderophore exporter MmpL5,Green fluorescent protein

Aequorea victoria

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 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–493 Chain D; UniProt 688–964 Not recorded Meromycolate extension acyl carrier protein × 1 (A0R0B3) ELECTRON MICROSCOPY cryo-EM buffer:pH 8;50 mM HEPES pH8.0, 150 mM NaCl, 0.004% LMNG, 50 uM Bedaquiline cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 D; PDBConstruct 1–493; UniProt 1–493 Author chain D; PDBConstruct 494–770; UniProt 688–964

Meromycolate extension acyl carrier protein

OrganismNot specified

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 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain I; UniProt 3–80 Not recorded Siderophore exporter MmpL5,Green fluorescent protein × 1 (P9WJV1,P42212) ELECTRON MICROSCOPY cryo-EM buffer:pH 8;50 mM HEPES pH8.0, 150 mM NaCl, 0.004% LMNG, 50 uM Bedaquiline cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 I; PDBConstruct 1–78; UniProt 3–80

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 9s2u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9s2u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9s2u
Deposition date deposition_date2025-07-22
最后修订 last_revision2025-10-08
Structure title title1:1 complex of M.tuberculosis MmpL5 and M.smegmatis AcpM
Keywords keywordsDrug Efflux, RND transporter, Tuberculosis, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier32.82
Radius of gyration Rg (electron density) rg_electron32.52
Forward intensity I(0) i0108182000.00
Molecular weight molecular_weight87458.0 kDa
Excluded volume excluded_volume111530 ų
Envelope volume envelope_volume135970 ų
Hydration-shell volume shell_volume36574 ų
Envelope diameter envelope_diameter125.0
Shell Rg shell_rg37.40
Envelope Rg envelope_rg33.10
Shape Rg shape_rg32.57
Total Rg total_rg32.74
Total atoms total_atoms6157
Residues n_residues816
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 dmax117.2
Rg (real space) rg_real33.19
Rg uncertainty (real space) rg_real_error1.34
I(0) (real space) i0_real1.0820e+08
I(0) uncertainty (real space) i0_real_error1.8490e+06
Rg (reciprocal space) rg_reciprocal33.04
I(0) (reciprocal space) i0_reciprocal108200000.0000
Solution quality estimate total_estimate0.8076
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.3
Skewness Skewness skewness0.574
Kurtosis Kurtosis kurtosis-0.242
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha35210000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.628; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.685; Smooth: 0.927

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)