1fbd

CRYSTALLOGRAPHIC STUDIES OF THE CATALYTIC MECHANISM OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE

Method: X-RAY DIFFRACTION Dmax: 89.1 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 1–335 Chain B; UniProt 1–335 Not recorded MN MANGANESE (II) ION × 8 AHG 2,5-anhydro-1,6-di-O-phosphono-D-glucitol × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.90 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.

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 1–335; UniProt 1–335 Author chain B; PDBConstruct 1–335; UniProt 1–335

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 1fbd

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1fbd
Deposition date deposition_date1992-10-16
Structure title titleCRYSTALLOGRAPHIC STUDIES OF THE CATALYTIC MECHANISM OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE
Keywords keywordsHYDROLASE(PHOSPHORIC MONOESTER); HYDROLASE(PHOSPHORIC MONOESTER)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.58
Radius of gyration Rg (electron density) rg_electron25.60
Forward intensity I(0) i076592600.00
Molecular weight molecular_weight69291.0 kDa
Excluded volume excluded_volume87179 ų
Envelope volume envelope_volume102430 ų
Hydration-shell volume shell_volume32736 ų
Envelope diameter envelope_diameter93.5
Shell Rg shell_rg33.34
Envelope Rg envelope_rg25.96
Shape Rg shape_rg25.62
Total Rg total_rg26.35
Total atoms total_atoms5909
Residues n_residues628
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 dmax89.1
Rg (real space) rg_real26.53
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real7.6590e+07
I(0) uncertainty (real space) i0_real_error1.1530e+06
Rg (reciprocal space) rg_reciprocal26.55
I(0) (reciprocal space) i0_reciprocal76590000.0000
Solution quality estimate total_estimate0.8819
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.7
Skewness Skewness skewness0.323
Kurtosis Kurtosis kurtosis-0.367
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha26150000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.832; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.976

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1fbda_
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_idd1fbdb_
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_id1fbdA01
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_id1fbdA02
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_id1fbdB01
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_id1fbdB02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily80

8. Citations (2)

9. Files and Curves (10)