7bwr

Mycobacterium smegmatis arabinosyltransferase complex EmbB2-AcpM2 in substrate DPA bound asymmetric "active state"

Method: ELECTRON MICROSCOPY Dmax: 138.2 Å Quality: GOOD

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

Integral membrane indolylacetylinositol arabinosyltransferase EmbB

Mycolicibacterium smegmatis MC2 155

UniProt I7GAQ2

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–1082 Chain B; UniProt 1–1082 Not recorded Meromycolate extension acyl carrier protein × 2 (A0R0B3) CA CALCIUM ION × 1 F8L [(2Z,6E,10E,14Z,18E,22Z,26Z)-3,7,11,15,19,23,27,31,35,39-decamethyltetraconta-2,6,10,14,18,22,26,30,34,38-decaenyl] [(2S,3S,4S,5R)-5-(hydroxymethyl)-3,4-bis(oxidanyl)oxolan-2-yl] hydrogen phosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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 I7GAQ2_MYCS2
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1082; UniProt 1–1082 Author chain B; PDBConstruct 1–1082; UniProt 1–1082

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–99 Chain D; UniProt 1–99 Not recorded Integral membrane indolylacetylinositol arabinosyltransferase EmbB × 2 (I7GAQ2) CA CALCIUM ION × 1 F8L [(2Z,6E,10E,14Z,18E,22Z,26Z)-3,7,11,15,19,23,27,31,35,39-decamethyltetraconta-2,6,10,14,18,22,26,30,34,38-decaenyl] [(2S,3S,4S,5R)-5-(hydroxymethyl)-3,4-bis(oxidanyl)oxolan-2-yl] hydrogen phosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

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 C; PDBConstruct 1–99; UniProt 1–99 Author chain D; 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 7bwr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7bwr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7bwr
Deposition date deposition_date2020-04-15
Structure title titleMycobacterium smegmatis arabinosyltransferase complex EmbB2-AcpM2 in substrate DPA bound asymmetric "active state"
Keywords keywords;Mycobacterium tuberculosis, EmbB, cryo-EM, ethambutol, cell wall synthesis, arabinoglacatan, arabinosyltransferase, acyl-carrier-protein, TRANSFERASE ;; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.83
Radius of gyration Rg (electron density) rg_electron41.98
Forward intensity I(0) i0602550000.00
Molecular weight molecular_weight204590.0 kDa
Excluded volume excluded_volume257530 ų
Envelope volume envelope_volume381120 ų
Hydration-shell volume shell_volume73872 ų
Envelope diameter envelope_diameter140.0
Shell Rg shell_rg48.52
Envelope Rg envelope_rg41.37
Shape Rg shape_rg42.00
Total Rg total_rg42.27
Total atoms total_atoms14450
Residues n_residues2064
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 dmax138.2
Rg (real space) rg_real42.66
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real6.0250e+08
I(0) uncertainty (real space) i0_real_error1.0860e+07
Rg (reciprocal space) rg_reciprocal42.83
I(0) (reciprocal space) i0_reciprocal602700000.0000
Solution quality estimate total_estimate0.8230
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.0
Skewness Skewness skewness0.171
Kurtosis Kurtosis kurtosis-0.459
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha56340000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.902; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)