6as9

Filamentous Assembly of Green Fluorescent Protein Supported by a C-terminal fusion of 18-residues, viewed in space group P212121 form 2

Method: X-RAY DIFFRACTION Dmax: 78.1 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 homooligomer Homooligomer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–238 Non-standard monomer:Yes (specific site not provided by mmCIF) ACT ACETATE ION × 10 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 10 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;277 K;0.1 M sodium acetate, pH 5.0 and 65% (v/v) 2-methyl-2,4-pentanediol Resolution 1.75 Å R-free 0.183

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 6as9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6as9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6as9
Deposition date deposition_date2017-08-23
Structure title titleFilamentous Assembly of Green Fluorescent Protein Supported by a C-terminal fusion of 18-residues, viewed in space group P212121 form 2
Keywords keywordsfilament, protofilament, 2 sub 1 screw symmetry, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.33
Radius of gyration Rg (electron density) rg_electron19.42
Forward intensity I(0) i013701400.00
Molecular weight molecular_weight28022.0 kDa
Excluded volume excluded_volume35134 ų
Envelope volume envelope_volume41795 ų
Hydration-shell volume shell_volume18677 ų
Envelope diameter envelope_diameter80.8
Shell Rg shell_rg25.17
Envelope Rg envelope_rg20.68
Shape Rg shape_rg19.36
Total Rg total_rg20.43
Total atoms total_atoms1976
Residues n_residues244
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 dmax78.1
Rg (real space) rg_real20.46
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real1.3700e+07
I(0) uncertainty (real space) i0_real_error1.8110e+05
Rg (reciprocal space) rg_reciprocal20.43
I(0) (reciprocal space) i0_reciprocal13700000.0000
Solution quality estimate total_estimate0.7827
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.4
Skewness Skewness skewness0.688
Kurtosis Kurtosis kurtosis0.577
Angular range angular_range— – 0.3900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3110000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.457; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.834; Smooth: 0.965

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd6as9a1
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_idd6as9a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

8. Citations (1)

9. Files and Curves (10)