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1c81

MICHAELIS COMPLEX OF FRUCTOSE-2,6-BISPHOSPHATASE

Method: X-RAY DIFFRACTION Dmax: 59.5 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

FRUCTOSE-2,6-BISPHOSPHATASE

Rattus norvegicus

UniProt P07953

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 251–440 Not recorded FDQ 2,5-anhydro-1-deoxy-1-phosphono-6-O-phosphono-D-glucitol × 2 X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；pH 7.25；293 K；PEG 4000, sodium chloride, Hepes, pH 7.25, EVAPORATION, temperature 293.0K Resolution 2.50 Å R-free 0.287

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.

Other PDB Difference from Current Entry 1C81 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1C7Z REGULATORY COMPLEX OF FRUCTOSE-2,6-BISPHOSPHATASE Deposited 2000-04-03 Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 251–440（190 aa）
Chain B 251–440（190 aa）
Not recorded PO4 PHOSPHATE ION × 2 G3H GLYCERALDEHYDE-3-PHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 7.25；293 K；PEG 4000, sodium chloride, Hepes, pH 7.25, EVAPORATION, temperature 293.0K
Resolution 2.60 Å R-free 0.253
1C80 REGULATORY COMPLEX OF FRUCTOSE-2,6-BISPHOSPHATASE Deposited 2000-04-03 Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 251–440（190 aa）
Chain B 251–440（190 aa）
Not recorded PO4 PHOSPHATE ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 7.25；293 K；PEG 4000, sodium chloride, Hepes, pH 7.25, EVAPORATION, temperature 293.0K
Resolution 2.20 Å R-free 0.265
1FBT THE BISPHOSPHATASE DOMAIN OF THE BIFUNCTIONAL RAT LIVER 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE Deposited 1996-03-08 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 251–440（190 aa）
Chain B 251–440（190 aa）
Mutation：30 AMINO ACIDS DELETED FROM THE C-TERMINAL Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：30 AMINO ACIDS DELETED FROM THE C-TERMINAL Non-standard monomer：Yes (specific site not provided by mmCIF) PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å R-free 0.278
1TIP THE BISPHOSPHATASE DOMAIN OF THE BIFUNCTIONAL RAT LIVER 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE Deposited 1997-05-28 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 251–440（190 aa）
Chain B 251–440（190 aa）
Mutation：30 C-TERMINAL AMINO ACIDS DELETED Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：30 C-TERMINAL AMINO ACIDS DELETED Non-standard monomer：Yes (specific site not provided by mmCIF) F6P 6-O-phosphono-beta-D-fructofuranose × 2 X-RAY DIFFRACTION
X-ray crystallization conditions A CATALYTIC PHOSPHOSENZYME INTERMEDIATE STATE OF THE BISPHOSPHATASE WAS PREPARED BY SOAKING OF THE NATIVE CRYSTAL OF THE PROTEIN AND TRAPPED USING THE CRYOGENIC DEVICE. A 2.2 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE INTERMEDIATE WAS DETERMINED. A PHOSPHORYLATED CATALYTIC HISTIDINE WAS VISUALIZED ALONG WITH THE FIRST PRODUCT, FRUCTOSE-6 - PHOSPHATE, AND THE CATALYTIC WATER, SHOWING THE COMPREHENSIVE GEOMETRY OF A TRIGONAL BI-PYRAMIDAL STRUCTURE.
Resolution 2.20 Å R-free 0.286

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name F261_RAT
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 2–191； UniProt 251–440

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 1c81

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1c81
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1c81
Deposition date deposition_date2000-04-03
Structure title titleMICHAELIS COMPLEX OF FRUCTOSE-2,6-BISPHOSPHATASE
Keywords keywordsRossmann fold, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier17.63 Å
Radius of gyration Rg (electron density) rg_electron16.60 Å
Forward intensity I(0) i09472390.00
Molecular weight molecular_weight22455.0 kDa
Excluded volume excluded_volume27939 ų
Envelope volume envelope_volume31651 ų
Hydration-shell volume shell_volume16019 ų
Envelope diameter envelope_diameter57.7 Å
Shell Rg shell_rg22.61 Å
Envelope Rg envelope_rg16.91 Å
Shape Rg shape_rg16.63 Å
Total Rg total_rg17.46 Å
Total atoms total_atoms1573
Residues n_residues191
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax59.5 Å
Rg (real space) rg_real17.56 Å
Rg uncertainty (real space) rg_real_error0.25 Å
I(0) (real space) i0_real9.4720e+06
I(0) uncertainty (real space) i0_real_error1.0670e+05
Rg (reciprocal space) rg_reciprocal17.57 Å
I(0) (reciprocal space) i0_reciprocal9472000.0000
Solution quality estimate total_estimate0.7112
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.4 Å
Skewness Skewness skewness0.259
Kurtosis Kurtosis kurtosis-0.308
Angular range angular_range— – 0.4500 Å−1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha2224000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.792; Stabil: 1.000; Sysdev: 0.291; Positv: 1.000; Valcen: 0.993; Smooth: 1.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1c81a_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.60 — Phosphoglycerate mutase-like
Superfamily Superfamily superfamilyc.60.1 — Phosphoglycerate mutase-like
Family Family familyc.60.1.4 — 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, phosphatase domain

CATH v4.4 (1 domains)

Domain ID domain_id1c81A00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1240 — Phosphoglycerate mutase-like
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8. Citations (2)

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9. Files and Curves (10)