8b6s

X-ray structure of the haloalkane dehalogenase HaloTag7 fusion to the green fluorescent protein GFP (ChemoG1) labeled with a chloroalkane tetramethylrhodamine fluorophore substrate

Method: X-RAY DIFFRACTION Dmax: 119.5 Å Quality: GOOD

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

Green fluorescent protein,Haloalkane dehalogenase

Rhodococcus sp.

UniProt P0A3G3

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 4–293 Non-standard monomer:Yes (specific site not provided by mmCIF) OEH [9-[2-carboxy-5-[2-[2-(6-chloranylhexoxy)ethoxy]ethylcarbamoyl]phenyl]-6-(dimethylamino)xanthen-3-ylidene]-dimethyl-azanium × 1 CL CHLORIDE ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.085 M Tris-HCl pH 8.5, 0.17 M sodium acetate, 15% (v/v) glycerol, 27% (m/v) PEG 4000 Resolution 1.80 Å R-free 0.201
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 4–293 Non-standard monomer:Yes (specific site not provided by mmCIF) OEH [9-[2-carboxy-5-[2-[2-(6-chloranylhexoxy)ethoxy]ethylcarbamoyl]phenyl]-6-(dimethylamino)xanthen-3-ylidene]-dimethyl-azanium × 1 CL CHLORIDE ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.085 M Tris-HCl pH 8.5, 0.17 M sodium acetate, 15% (v/v) glycerol, 27% (m/v) PEG 4000 Resolution 1.80 Å R-free 0.201

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.

41 other PDB entries and 72 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DHAA_RHOSO
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 236–525; UniProt 4–293 Author chain B; PDBConstruct 236–525; UniProt 4–293

Green fluorescent protein,Haloalkane dehalogenase

Rhodococcus sp.

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 3–238 Non-standard monomer:Yes (specific site not provided by mmCIF) OEH [9-[2-carboxy-5-[2-[2-(6-chloranylhexoxy)ethoxy]ethylcarbamoyl]phenyl]-6-(dimethylamino)xanthen-3-ylidene]-dimethyl-azanium × 1 CL CHLORIDE ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.085 M Tris-HCl pH 8.5, 0.17 M sodium acetate, 15% (v/v) glycerol, 27% (m/v) PEG 4000 Resolution 1.80 Å R-free 0.201
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 3–238 Non-standard monomer:Yes (specific site not provided by mmCIF) OEH [9-[2-carboxy-5-[2-[2-(6-chloranylhexoxy)ethoxy]ethylcarbamoyl]phenyl]-6-(dimethylamino)xanthen-3-ylidene]-dimethyl-azanium × 1 CL CHLORIDE ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.085 M Tris-HCl pH 8.5, 0.17 M sodium acetate, 15% (v/v) glycerol, 27% (m/v) PEG 4000 Resolution 1.80 Å R-free 0.201

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 743 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 2–235; UniProt 3–238 Author chain B; PDBConstruct 2–235; UniProt 3–238

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 8b6s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8b6s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8b6s
Deposition date deposition_date2022-09-27
Structure title titleX-ray structure of the haloalkane dehalogenase HaloTag7 fusion to the green fluorescent protein GFP (ChemoG1) labeled with a chloroalkane tetramethylrhodamine fluorophore substrate
Keywords keywords;haloalkane dehalogenase, HaloTag, HaloTag7, Self-Labeling Protein, green fluorescent protein, GFP, fluorophore, tetramethylerhodamine, TMR, HYDROLASE ;; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier35.66
Radius of gyration Rg (electron density) rg_electron34.94
Forward intensity I(0) i0205163000.00
Molecular weight molecular_weight118820.0 kDa
Excluded volume excluded_volume149810 ų
Envelope volume envelope_volume187970 ų
Hydration-shell volume shell_volume44395 ų
Envelope diameter envelope_diameter119.0
Shell Rg shell_rg41.70
Envelope Rg envelope_rg34.47
Shape Rg shape_rg34.92
Total Rg total_rg35.48
Total atoms total_atoms8405
Residues n_residues1033
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 dmax119.5
Rg (real space) rg_real35.63
Rg uncertainty (real space) rg_real_error1.06
I(0) (real space) i0_real2.0520e+08
I(0) uncertainty (real space) i0_real_error3.1430e+06
Rg (reciprocal space) rg_reciprocal35.65
I(0) (reciprocal space) i0_reciprocal205200000.0000
Solution quality estimate total_estimate0.8153
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary48.9
Skewness Skewness skewness0.245
Kurtosis Kurtosis kurtosis-0.502
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha93890000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.873; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id8b6sA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1820 — Alpha/Beta hydrolase fold, catalytic domain
Domain ID domain_id8b6sB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1820 — Alpha/Beta hydrolase fold, catalytic domain

8. Citations (1)

9. Files and Curves (10)