8smu

Integral fusion of the HtaA CR2 domain from Corynebacterium diphtheriae within EGFP

Method: X-RAY DIFFRACTION Dmax: 148.0 Å Quality: GOOD

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

HtaACR2 integral fusion within enhanced 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 Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–39 Chain A; UniProt 40–238 Non-standard monomer:Yes (specific site not provided by mmCIF) HEM PROTOPORPHYRIN IX CONTAINING FE × 1 GOL GLYCEROL × 7 1PE PENTAETHYLENE GLYCOL × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;298 K;1.9 M ammonium sulfate, 0.1 M sodium cacodylate trihydrate, 0.2 M sodium chloride Resolution 2.45 Å R-free 0.233
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–39 Chain B; UniProt 40–238 Non-standard monomer:Yes (specific site not provided by mmCIF) HEM PROTOPORPHYRIN IX CONTAINING FE × 1 GOL GLYCEROL × 4 1PE PENTAETHYLENE GLYCOL × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;298 K;1.9 M ammonium sulfate, 0.1 M sodium cacodylate trihydrate, 0.2 M sodium chloride Resolution 2.45 Å R-free 0.233
3 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 1–39 Chain C; UniProt 40–238 Non-standard monomer:Yes (specific site not provided by mmCIF) HEM PROTOPORPHYRIN IX CONTAINING FE × 1 GOL GLYCEROL × 7 1PE PENTAETHYLENE GLYCOL × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;298 K;1.9 M ammonium sulfate, 0.1 M sodium cacodylate trihydrate, 0.2 M sodium chloride Resolution 2.45 Å R-free 0.233
4 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 1–39 Chain D; UniProt 40–238 Non-standard monomer:Yes (specific site not provided by mmCIF) HEM PROTOPORPHYRIN IX CONTAINING FE × 1 GOL GLYCEROL × 5 1PE PENTAETHYLENE GLYCOL × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;298 K;1.9 M ammonium sulfate, 0.1 M sodium cacodylate trihydrate, 0.2 M sodium chloride Resolution 2.45 Å R-free 0.233

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 741 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 1–39; UniProt 1–39 Author chain A; PDBConstruct 207–403; UniProt 40–238 Author chain B; PDBConstruct 1–39; UniProt 1–39 Author chain B; PDBConstruct 207–403; UniProt 40–238 Author chain C; PDBConstruct 1–39; UniProt 1–39 Author chain C; PDBConstruct 207–403; UniProt 40–238 Author chain D; PDBConstruct 1–39; UniProt 1–39 Author chain D; PDBConstruct 207–403; UniProt 40–238

HtaACR2 integral fusion within enhanced green fluorescent protein

Aequorea victoria

UniProt Q6NIZ1

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 Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 344–507 Non-standard monomer:Yes (specific site not provided by mmCIF) HEM PROTOPORPHYRIN IX CONTAINING FE × 1 GOL GLYCEROL × 7 1PE PENTAETHYLENE GLYCOL × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;298 K;1.9 M ammonium sulfate, 0.1 M sodium cacodylate trihydrate, 0.2 M sodium chloride Resolution 2.45 Å R-free 0.233
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 344–507 Non-standard monomer:Yes (specific site not provided by mmCIF) HEM PROTOPORPHYRIN IX CONTAINING FE × 1 GOL GLYCEROL × 4 1PE PENTAETHYLENE GLYCOL × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;298 K;1.9 M ammonium sulfate, 0.1 M sodium cacodylate trihydrate, 0.2 M sodium chloride Resolution 2.45 Å R-free 0.233
3 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 344–507 Non-standard monomer:Yes (specific site not provided by mmCIF) HEM PROTOPORPHYRIN IX CONTAINING FE × 1 GOL GLYCEROL × 7 1PE PENTAETHYLENE GLYCOL × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;298 K;1.9 M ammonium sulfate, 0.1 M sodium cacodylate trihydrate, 0.2 M sodium chloride Resolution 2.45 Å R-free 0.233
4 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 344–507 Non-standard monomer:Yes (specific site not provided by mmCIF) HEM PROTOPORPHYRIN IX CONTAINING FE × 1 GOL GLYCEROL × 5 1PE PENTAETHYLENE GLYCOL × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;298 K;1.9 M ammonium sulfate, 0.1 M sodium cacodylate trihydrate, 0.2 M sodium chloride Resolution 2.45 Å R-free 0.233

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.

1 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q6NIZ1_CORDI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 43–206; UniProt 344–507 Author chain B; PDBConstruct 43–206; UniProt 344–507 Author chain C; PDBConstruct 43–206; UniProt 344–507 Author chain D; PDBConstruct 43–206; UniProt 344–507

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 8smu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8smu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8smu
Deposition date deposition_date2023-04-26
Structure title titleIntegral fusion of the HtaA CR2 domain from Corynebacterium diphtheriae within EGFP
Keywords keywordsHEME-BINDING DOMAIN, GREEN FLUORESCENT PROTEIN, INTEGRAL FUSION, FLUORESCENT PROTEIN; FLUORESCENT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier45.22
Radius of gyration Rg (electron density) rg_electron45.40
Forward intensity I(0) i0461273000.00
Molecular weight molecular_weight174740.0 kDa
Excluded volume excluded_volume217300 ų
Envelope volume envelope_volume293730 ų
Hydration-shell volume shell_volume56178 ų
Envelope diameter envelope_diameter151.4
Shell Rg shell_rg47.35
Envelope Rg envelope_rg44.44
Shape Rg shape_rg45.40
Total Rg total_rg45.52
Total atoms total_atoms12324
Residues n_residues1572
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 dmax148.0
Rg (real space) rg_real45.48
Rg uncertainty (real space) rg_real_error1.39
I(0) (real space) i0_real4.6130e+08
I(0) uncertainty (real space) i0_real_error8.4510e+06
Rg (reciprocal space) rg_reciprocal45.23
I(0) (reciprocal space) i0_reciprocal461100000.0000
Solution quality estimate total_estimate0.8341
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.5
Skewness Skewness skewness0.421
Kurtosis Kurtosis kurtosis-0.551
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25970000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.852; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.912; Smooth: 0.371

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)