1bk4

CRYSTAL STRUCTURE OF RABBIT LIVER FRUCTOSE-1,6-BISPHOSPHATASE AT 2.3 ANGSTROM RESOLUTION

Method: X-RAY DIFFRACTION Dmax: 72.8 Å Quality: GOOD

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

PROTEIN (FRUCTOSE-1,6-BISPHOSPHATASE)

OrganismNot specified

UniProt P00637

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 1–337 Not recorded MG MAGNESIUM ION × 4 SO4 SULFATE ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.4;10-15% PEG 4000, 50-200 MM A.S. IN 25 MM TRIS, pH 7.4 Resolution 2.30 Å
2 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–337 Not recorded MG MAGNESIUM ION × 4 SO4 SULFATE ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.4;10-15% PEG 4000, 50-200 MM A.S. IN 25 MM TRIS, pH 7.4 Resolution 2.30 Å

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name F16P_RABIT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–337; UniProt 1–337

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 1bk4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1bk4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1bk4
Deposition date deposition_date1998-07-14
Structure title titleCRYSTAL STRUCTURE OF RABBIT LIVER FRUCTOSE-1,6-BISPHOSPHATASE AT 2.3 ANGSTROM RESOLUTION
Keywords keywordsBISPHOSPHATASE, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.74
Radius of gyration Rg (electron density) rg_electron19.72
Forward intensity I(0) i019948500.00
Molecular weight molecular_weight34352.0 kDa
Excluded volume excluded_volume43258 ų
Envelope volume envelope_volume50313 ų
Hydration-shell volume shell_volume21286 ų
Envelope diameter envelope_diameter71.8
Shell Rg shell_rg26.33
Envelope Rg envelope_rg20.10
Shape Rg shape_rg19.73
Total Rg total_rg20.61
Total atoms total_atoms2404
Residues n_residues314
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 dmax72.8
Rg (real space) rg_real20.68
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real1.9950e+07
I(0) uncertainty (real space) i0_real_error2.4220e+05
Rg (reciprocal space) rg_reciprocal20.69
I(0) (reciprocal space) i0_reciprocal19950000.0000
Solution quality estimate total_estimate0.8570
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.3
Skewness Skewness skewness0.287
Kurtosis Kurtosis kurtosis-0.304
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5130000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.715; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1bk4a_
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.7 — Carbohydrate phosphatase
Superfamily Superfamily superfamilye.7.1 — Carbohydrate phosphatase
Family Family familye.7.1.1 — Inositol monophosphatase/fructose-1,6-bisphosphatase-like

CATH v4.4 (2 domains)

Domain ID domain_id1bk4A01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology540 — Fructose-1,6-Bisphosphatase; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Fructose-1,6-Bisphosphatase, subunit A, domain 1
Domain ID domain_id1bk4A02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily80

8. Citations (1)

9. Files and Curves (10)