4gwy

Crystal Structure of AMP Complexes of Porcine Liver Fructose-1,6-bisphosphatase with Blocked Subunit Pair Rotation

Method: X-RAY DIFFRACTION Dmax: 73.1 Å Quality: GOOD

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

Fructose-1,6-bisphosphatase 1

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 2–338 Mutation:M18K F6P 6-O-phosphono-beta-D-fructofuranose × 4 PO4 PHOSPHATE ION × 4 MG MAGNESIUM ION × 12 AMP ADENOSINE MONOPHOSPHATE × 4 X-RAY DIFFRACTION X-ray crystallization conditions:HANGING DROP;pH 7.5;298 K;PEG3350, t-butyl alcohol, glycerol, pH 7.5, HANGING DROP, temperature 298K Resolution 3.00 Å R-free 0.266

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 F16P1_PIG
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–337; UniProt 2–338

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 4gwy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4gwy
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4gwy
Deposition date deposition_date2012-09-03
Structure title titleCrystal Structure of AMP Complexes of Porcine Liver Fructose-1,6-bisphosphatase with Blocked Subunit Pair Rotation
Keywords keywordsallosteric enzymes, AMP inhibition, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.54
Radius of gyration Rg (electron density) rg_electron19.55
Forward intensity I(0) i022314800.00
Molecular weight molecular_weight36242.0 kDa
Excluded volume excluded_volume45524 ų
Envelope volume envelope_volume51652 ų
Hydration-shell volume shell_volume21835 ų
Envelope diameter envelope_diameter72.8
Shell Rg shell_rg26.40
Envelope Rg envelope_rg19.92
Shape Rg shape_rg19.57
Total Rg total_rg20.40
Total atoms total_atoms2536
Residues n_residues326
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 dmax73.1
Rg (real space) rg_real20.46
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real2.2310e+07
I(0) uncertainty (real space) i0_real_error3.0680e+05
Rg (reciprocal space) rg_reciprocal20.47
I(0) (reciprocal space) i0_reciprocal22320000.0000
Solution quality estimate total_estimate0.8511
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.4
Skewness Skewness skewness0.242
Kurtosis Kurtosis kurtosis-0.321
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5465000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.690; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4gwya_
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_id4gwyA01
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_id4gwyA02
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)