4ogs

Crystal structure of GFP S205A/T203V at 2.2 A resolution

Method: X-RAY DIFFRACTION Dmax: 78.7 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–238 Mutation:S205A, T203V Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.8;298 K;Crystals were produced using 1 uL protein (26 mg/ml in 0.1 M imidazole, pH 7.8) mixed with 1 uL well solution, Crystallization screens varied from 22% to 32% (w:v) polyethylene glycol monomethyl ether (PEG) 2000 and 0.05M to 0.2M KBr at room temperature, for a range of pH values near neutrality, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.21 Å R-free 0.306
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–238 Mutation:S205A, T203V Non-standard monomer:Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.8;298 K;Crystals were produced using 1 uL protein (26 mg/ml in 0.1 M imidazole, pH 7.8) mixed with 1 uL well solution, Crystallization screens varied from 22% to 32% (w:v) polyethylene glycol monomethyl ether (PEG) 2000 and 0.05M to 0.2M KBr at room temperature, for a range of pH values near neutrality, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.21 Å R-free 0.306

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 1–236; UniProt 1–238 Author chain B; 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 4ogs

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4ogs
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4ogs
Deposition date deposition_date2014-01-16
Structure title titleCrystal structure of GFP S205A/T203V at 2.2 A resolution
Keywords keywordsbeta-can, 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_guinier23.32
Radius of gyration Rg (electron density) rg_electron22.18
Forward intensity I(0) i041557200.00
Molecular weight molecular_weight49768.0 kDa
Excluded volume excluded_volume62067 ų
Envelope volume envelope_volume71652 ų
Hydration-shell volume shell_volume26455 ų
Envelope diameter envelope_diameter80.1
Shell Rg shell_rg29.37
Envelope Rg envelope_rg22.33
Shape Rg shape_rg22.17
Total Rg total_rg23.04
Total atoms total_atoms3520
Residues n_residues450
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 dmax78.7
Rg (real space) rg_real23.22
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real4.1560e+07
I(0) uncertainty (real space) i0_real_error5.6210e+05
Rg (reciprocal space) rg_reciprocal23.24
I(0) (reciprocal space) i0_reciprocal41560000.0000
Solution quality estimate total_estimate0.8039
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.9
Skewness Skewness skewness0.223
Kurtosis Kurtosis kurtosis-0.434
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10390000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.816; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4ogsa_
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_idd4ogsb_
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 (2 domains)

Domain ID domain_id4ogsA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily10 — Green fluorescent protein
Domain ID domain_id4ogsB00
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)