1fj9

FRUCTOSE-1,6-BISPHOSPHATASE (MUTANT Y57W) PRODUCTS/ZN/AMP COMPLEX (T-STATE)

Method: X-RAY DIFFRACTION Dmax: 90.2 Å Quality: GOOD

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

FRUCTOSE-1,6-BISPHOSPHATASE

Sus scrofa

UniProt P00636

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 Chain B; UniProt 1–337 Mutation:Y57W F6P 6-O-phosphono-beta-D-fructofuranose × 4 ZN ZINC ION × 8 PO4 PHOSPHATE ION × 4 AMP ADENOSINE MONOPHOSPHATE × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;300 K;PEG3350, MPD, Hepes, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 300K Resolution 2.50 Å R-free 0.258

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.

66 other PDB entries and 79 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name F16P_PIG
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–337; UniProt 1–337 Author chain B; 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 1fj9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1fj9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1fj9
Deposition date deposition_date2000-08-07
Structure title titleFRUCTOSE-1,6-BISPHOSPHATASE (MUTANT Y57W) PRODUCTS/ZN/AMP COMPLEX (T-STATE)
Keywords keywordsBisphosphatase, allosteric enzymes, gluconeogenesis, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.54
Radius of gyration Rg (electron density) rg_electron25.50
Forward intensity I(0) i081719400.00
Molecular weight molecular_weight71251.0 kDa
Excluded volume excluded_volume89380 ų
Envelope volume envelope_volume102830 ų
Hydration-shell volume shell_volume32914 ų
Envelope diameter envelope_diameter92.6
Shell Rg shell_rg33.49
Envelope Rg envelope_rg25.79
Shape Rg shape_rg25.52
Total Rg total_rg26.24
Total atoms total_atoms4974
Residues n_residues638
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 dmax90.2
Rg (real space) rg_real26.48
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real8.1720e+07
I(0) uncertainty (real space) i0_real_error1.1820e+06
Rg (reciprocal space) rg_reciprocal26.50
I(0) (reciprocal space) i0_reciprocal81720000.0000
Solution quality estimate total_estimate0.8782
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.1
Skewness Skewness skewness0.299
Kurtosis Kurtosis kurtosis-0.399
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22250000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.810; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1fj9a_
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
Domain ID domain_idd1fj9b_
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 (4 domains)

Domain ID domain_id1fj9A01
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_id1fj9A02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily80
Domain ID domain_id1fj9B01
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_id1fj9B02
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)