5jzl

The Structure of Monomeric Ultra Stable Green Fluorescent Protein

Method: X-RAY DIFFRACTION Dmax: 84.4 Å Quality: GOOD

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

Green fluorescent protein

Aequorea victoria

UniProt A0A059PIQ0

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 3–238 Fragment:UNP residues 3-238 Non-standard monomer:Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;281 K;22% w/v PEG 8000, 0.2 M sodium chloride, 0.1 M phosphate-citrate buffer pH 3.7, 4% v/v acetone Resolution 1.80 Å R-free 0.217
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 3–238 Fragment:UNP residues 3-238 Non-standard monomer:Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 1 NA SODIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;281 K;22% w/v PEG 8000, 0.2 M sodium chloride, 0.1 M phosphate-citrate buffer pH 3.7, 4% v/v acetone Resolution 1.80 Å R-free 0.217

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.

91 other PDB entries and 136 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A059PIQ0_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 14–247; UniProt 3–238 Author chain B; PDBConstruct 14–247; UniProt 3–238

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 5jzl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5jzl
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5jzl
Deposition date deposition_date2016-05-17
Structure title titleThe Structure of Monomeric Ultra Stable Green Fluorescent Protein
Keywords keywordsgreen fluorescent protein, GFP, thermostable, monomeric, 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_guinier25.42
Radius of gyration Rg (electron density) rg_electron24.51
Forward intensity I(0) i045545700.00
Molecular weight molecular_weight52168.0 kDa
Excluded volume excluded_volume65166 ų
Envelope volume envelope_volume77007 ų
Hydration-shell volume shell_volume26511 ų
Envelope diameter envelope_diameter88.0
Shell Rg shell_rg31.33
Envelope Rg envelope_rg24.63
Shape Rg shape_rg24.49
Total Rg total_rg25.32
Total atoms total_atoms3677
Residues n_residues461
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 dmax84.4
Rg (real space) rg_real25.43
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real4.5550e+07
I(0) uncertainty (real space) i0_real_error6.8720e+05
Rg (reciprocal space) rg_reciprocal25.43
I(0) (reciprocal space) i0_reciprocal45550000.0000
Solution quality estimate total_estimate0.8846
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.2
Skewness Skewness skewness0.363
Kurtosis Kurtosis kurtosis-0.393
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14060000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.857; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.941

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd5jzla1
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_idd5jzla2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd5jzlb1
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_idd5jzlb2
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_id5jzlA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily10 — Green fluorescent protein
Domain ID domain_id5jzlB00
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)