1w7s

Wild-Type Aequorea victoria Green Fluorescent Protein

Method: X-RAY DIFFRACTION Dmax: 90.5 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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–238 Chain B; UniProt 1–238 Chain C; UniProt 1–238 Chain D; UniProt 1–238 Mutation:YES Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.8;277 K;CRYSTALS WERE GROWN AT 4C FROM 50 MM MGCL2, 14-17 % PEG3350 AND 50-100 MM TRIS/CL PH 7.8 - 8.6. Resolution 1.85 Å R-free 0.216

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 Author chain B; PDBConstruct 1–236; UniProt 1–238 Author chain C; PDBConstruct 1–236; UniProt 1–238 Author chain D; 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 1w7s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1w7s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1w7s
Deposition date deposition_date2004-09-09
Structure title titleWild-Type Aequorea victoria Green Fluorescent Protein
Keywords keywordsLUMINESCENT PROTEIN, BIOLUMINIESCENCE, FLUORESCENT PROTEIN, BETA-BARREL, BIOLUMINESCENCE; LUMINESCENT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.81
Radius of gyration Rg (electron density) rg_electron28.84
Forward intensity I(0) i0170060000.00
Molecular weight molecular_weight103530.0 kDa
Excluded volume excluded_volume129470 ų
Envelope volume envelope_volume155180 ų
Hydration-shell volume shell_volume43355 ų
Envelope diameter envelope_diameter93.8
Shell Rg shell_rg37.39
Envelope Rg envelope_rg28.68
Shape Rg shape_rg28.81
Total Rg total_rg29.70
Total atoms total_atoms7314
Residues n_residues907
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 dmax90.5
Rg (real space) rg_real29.87
Rg uncertainty (real space) rg_real_error0.18
I(0) (real space) i0_real1.6550e+08
I(0) uncertainty (real space) i0_real_error1.8920e+06
Rg (reciprocal space) rg_reciprocal29.72
I(0) (reciprocal space) i0_reciprocal170100000.0000
Solution quality estimate total_estimate0.7230
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary37.6
Skewness Skewness skewness0.205
Kurtosis Kurtosis kurtosis-0.418
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha5.0680
Highest regularization parameter α highest_alpha58400000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.953; Stabil: 0.925; Sysdev: 0.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.800

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1w7sa_
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_idd1w7sb_
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_idd1w7sc_
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_idd1w7sd_
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 (4 domains)

Domain ID domain_id1w7sA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily10 — Green fluorescent protein
Domain ID domain_id1w7sB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily10 — Green fluorescent protein
Domain ID domain_id1w7sC00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily10 — Green fluorescent protein
Domain ID domain_id1w7sD00
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)