2h9w

Green fluorescent protein ground states: the influence of a second protonation site near the chromophore

Method: X-RAY DIFFRACTION Dmax: 50.4 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 2–237 Non-standard monomer:Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;298 K;AS, Tris, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.82 Å R-free 0.186

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 5–238; UniProt 2–237

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 2h9w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2h9w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2h9w
Deposition date deposition_date2006-06-12
Structure title titleGreen fluorescent protein ground states: the influence of a second protonation site near the chromophore
Keywords keywordsGFP, CHROMOPHORE, MUTANT, FLUORESCENT, pH, BIOSENSOR, CHLORIDE, HALIDE, HALOGEN, LUMINESCENT PROTEIN; LUMINESCENT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.20
Radius of gyration Rg (electron density) rg_electron18.03
Forward intensity I(0) i013457200.00
Molecular weight molecular_weight27270.0 kDa
Excluded volume excluded_volume34047 ų
Envelope volume envelope_volume40008 ų
Hydration-shell volume shell_volume18520 ų
Envelope diameter envelope_diameter66.7
Shell Rg shell_rg24.57
Envelope Rg envelope_rg18.81
Shape Rg shape_rg18.01
Total Rg total_rg19.10
Total atoms total_atoms1922
Residues n_residues236
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 dmax50.4
Rg (real space) rg_real18.40
Rg uncertainty (real space) rg_real_error0.05
I(0) (real space) i0_real1.2900e+07
I(0) uncertainty (real space) i0_real_error9.5890e+04
Rg (reciprocal space) rg_reciprocal19.17
I(0) (reciprocal space) i0_reciprocal13460000.0000
Solution quality estimate total_estimate0.6864
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary23.1
Skewness Skewness skewness0.181
Kurtosis Kurtosis kurtosis-0.438
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha2.2960
Highest regularization parameter α highest_alpha3283000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.989; Stabil: 0.988; Sysdev: 0.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2h9wa1
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_idd2h9wa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2h9wA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily10 — Green fluorescent protein

8. Citations (2)

9. Files and Curves (10)