2qle

GFP/S205V mutant

Method: X-RAY DIFFRACTION Dmax: 102.1 Å Quality: REASONABLE

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

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 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–238 Mutation:Q80R, S205V Non-standard monomer:Yes (specific site not provided by mmCIF) IMD IMIDAZOLE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;298 K;100mM Imidazol pH 8.0, 1.1M Na Citrate at room temperature for 6-7 months., temperature 298K Resolution 1.59 Å R-free 0.256
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–238 Mutation:Q80R, S205V Non-standard monomer:Yes (specific site not provided by mmCIF) IMD IMIDAZOLE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;298 K;100mM Imidazol pH 8.0, 1.1M Na Citrate at room temperature for 6-7 months., temperature 298K Resolution 1.59 Å R-free 0.256
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 1–238 Mutation:Q80R, S205V Non-standard monomer:Yes (specific site not provided by mmCIF) IMD IMIDAZOLE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;298 K;100mM Imidazol pH 8.0, 1.1M Na Citrate at room temperature for 6-7 months., temperature 298K Resolution 1.59 Å R-free 0.256
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 1–238 Mutation:Q80R, S205V Non-standard monomer:Yes (specific site not provided by mmCIF) IMD IMIDAZOLE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;298 K;100mM Imidazol pH 8.0, 1.1M Na Citrate at room temperature for 6-7 months., temperature 298K Resolution 1.59 Å R-free 0.256

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 1–236; UniProt 1–238 Author chain B; PDBConstruct 1–236; UniProt 1–238 Author chain C; PDBConstruct 1–236; UniProt 1–238 Author chain D; PDBConstruct 1–236; UniProt 1–238

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 2qle

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2qle
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2qle
Deposition date deposition_date2007-07-12
Structure title titleGFP/S205V mutant
Keywords keywordsGFP mutant, alternative excited state proton transfer pathway, 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_guinier32.13
Radius of gyration Rg (electron density) rg_electron31.40
Forward intensity I(0) i0154427000.00
Molecular weight molecular_weight99174.0 kDa
Excluded volume excluded_volume123860 ų
Envelope volume envelope_volume149890 ų
Hydration-shell volume shell_volume40161 ų
Envelope diameter envelope_diameter106.5
Shell Rg shell_rg37.91
Envelope Rg envelope_rg31.20
Shape Rg shape_rg31.40
Total Rg total_rg31.95
Total atoms total_atoms7020
Residues n_residues901
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 dmax102.1
Rg (real space) rg_real32.03
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real1.5440e+08
I(0) uncertainty (real space) i0_real_error2.3040e+06
Rg (reciprocal space) rg_reciprocal32.08
I(0) (reciprocal space) i0_reciprocal154400000.0000
Solution quality estimate total_estimate0.7277
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary41.7
Skewness Skewness skewness0.206
Kurtosis Kurtosis kurtosis-0.550
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha61810000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.939; Stabil: 1.000; Sysdev: 0.242; Positv: 1.000; Valcen: 1.000; Smooth: 0.911

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (5 domains)

Domain ID domain_idd2qlea1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.22 — GFP-like
Superfamily Superfamily superfamilyd.22.1 — GFP-like
Family Family familyd.22.1.1 — Fluorescent proteins
Domain ID domain_idd2qlea2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2qleb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.22 — GFP-like
Superfamily Superfamily superfamilyd.22.1 — GFP-like
Family Family familyd.22.1.1 — Fluorescent proteins
Domain ID domain_idd2qlec_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.22 — GFP-like
Superfamily Superfamily superfamilyd.22.1 — GFP-like
Family Family familyd.22.1.1 — Fluorescent proteins
Domain ID domain_idd2qled_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.22 — GFP-like
Superfamily Superfamily superfamilyd.22.1 — GFP-like
Family Family familyd.22.1.1 — Fluorescent proteins

CATH v4.4 (4 domains)

Domain ID domain_id2qleA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily10 — Green fluorescent protein
Domain ID domain_id2qleB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily10 — Green fluorescent protein
Domain ID domain_id2qleC00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily10 — Green fluorescent protein
Domain ID domain_id2qleD00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily10 — Green fluorescent protein

8. Citations (1)

9. Files and Curves (10)