3g9a

Green fluorescent protein bound to minimizer nanobody

Method: X-RAY DIFFRACTION Dmax: 75.6 Å Quality: GOOD

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–238 Mutation:S2G, Q80R, F99S, M153T, V163A Non-standard monomer:Yes (specific site not provided by mmCIF) Minimizer × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6.5;293 K;100mM Mes pH 6.5, 30% PEG 8000, 15% Glycerol, VAPOR DIFFUSION, temperature 293K Resolution 1.61 Å R-free 0.194

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 A; 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 3g9a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3g9a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3g9a
Deposition date deposition_date2009-02-13
Structure title titleGreen fluorescent protein bound to minimizer nanobody
Keywords keywordsAntibody Complex, Chromophore, Luminescence, Photoprotein, FLUORESCENT PROTEIN-IMMUNE SYSTEM COMPLEX, NANOBODY; FLUORESCENT PROTEIN/IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.23
Radius of gyration Rg (electron density) rg_electron21.26
Forward intensity I(0) i027420100.00
Molecular weight molecular_weight39329.0 kDa
Excluded volume excluded_volume48855 ų
Envelope volume envelope_volume56482 ų
Hydration-shell volume shell_volume22383 ų
Envelope diameter envelope_diameter78.2
Shell Rg shell_rg27.83
Envelope Rg envelope_rg21.48
Shape Rg shape_rg21.22
Total Rg total_rg22.18
Total atoms total_atoms2770
Residues n_residues337
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 dmax75.6
Rg (real space) rg_real22.20
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real2.7420e+07
I(0) uncertainty (real space) i0_real_error4.0000e+05
Rg (reciprocal space) rg_reciprocal22.21
I(0) (reciprocal space) i0_reciprocal27420000.0000
Solution quality estimate total_estimate0.8041
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.2
Skewness Skewness skewness0.326
Kurtosis Kurtosis kurtosis-0.348
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7389000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.820; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd3g9aa_
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_idd3g9ab1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd3g9ab2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id3g9aA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily10 — Green fluorescent protein
Domain ID domain_id3g9aB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)