← Back to search
1fpd

STRUCTURAL ASPECTS OF THE ALLOSTERIC INHIBITION OF FRUCTOSE-1,6-BISPHOSPHATASE BY AMP: THE BINDING OF BOTH THE SUBSTRATE ANALOGUE 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND CATALYTIC METAL IONS MONITORED BY X-RAY CRYSTALLOGRAPHY

Method: X-RAY DIFFRACTION
▼

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

FRUCTOSE 1,6-BISPHOSPHATASE

Sus scrofa

UniProt P00636

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 4 MANGANESE (II) ION × 8 2,5-anhydro-1,6-di-O-phosphono-D-glucitol × 4 ADENOSINE MONOPHOSPHATE × 4 water × 4 Consistent with protein count

Other States of the Same Protein in the Database

Monomer
1nuw 1nux 1nuy 1nuz 1nv0 1nv1 1nv2 1nv3 1nv4 1nv5 1nv6

11 assemblies

Homodimer
1nv7 1q9d

2 assemblies

Homotetramer
1cnq 1eyi 1eyj 1eyk 1fbc 1fbd 1fbe 1fbf 1fbg 1fbh 1fbp 1fj6

67 assemblies; showing the first 12

Other homooligomers

None

Heteromeric or nucleic-acid complex

None

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id1fpd
Deposition date deposition_date1994-12-15
Structure title titleSTRUCTURAL ASPECTS OF THE ALLOSTERIC INHIBITION OF FRUCTOSE-1,6-BISPHOSPHATASE BY AMP: THE BINDING OF BOTH THE SUBSTRATE ANALOGUE 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND CATALYTIC METAL IONS MONITORED BY X-RAY CRYSTALLOGRAPHY
Keywords keywordsHYDROLASE (PHOSPHORIC MONOESTER); HYDROLASE (PHOSPHORIC MONOESTER)
Experimental Method methodX-RAY DIFFRACTION
▼

3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1fpd__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1fpd__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1fpd__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg（Guinier）34.48 Å
Rg (electron density)33.73 Å
Total Rg34.08 Å
Atom count12064
Residues1268
Excluded volume177690 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1fpd__assembly_1__model_1 tetrameric （4） Success 4.1.3-1-20251215 (887e7ef) View Download
▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (5)

▼

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1fpda_
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_idd1fpdb_
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_id1fpdA01
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_id1fpdA02
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_id1fpdB01
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_id1fpdB02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily80 —
▶

7. Citations (4)