1lev

PORCINE KIDNEY FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH AN AMP-SITE INHIBITOR

Method: X-RAY DIFFRACTION Dmax: 85.5 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 F; UniProt 1–337 Not recorded F6P 6-O-phosphono-beta-D-fructofuranose × 4 MN MANGANESE (II) ION × 8 CLI 3-(2-CARBOXY-ETHYL)-4,6-DICHLORO-1H-INDOLE-2-CARBOXYLIC ACID × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;0.2M Na Acetate, 13.75% PEG 4000, 0.1M Hepes pH7.0, 1mM F6P, 2mM MnCl2, 1mM inhibitor, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 2.15 Å R-free 0.255

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 F; 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 1lev

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1lev
Deposition date deposition_date2002-04-10
Structure title titlePORCINE KIDNEY FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH AN AMP-SITE INHIBITOR
Keywords keywordsHydrolase; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.37
Radius of gyration Rg (electron density) rg_electron25.39
Forward intensity I(0) i076353800.00
Molecular weight molecular_weight69415.0 kDa
Excluded volume excluded_volume87337 ų
Envelope volume envelope_volume99840 ų
Hydration-shell volume shell_volume32292 ų
Envelope diameter envelope_diameter91.6
Shell Rg shell_rg33.01
Envelope Rg envelope_rg25.61
Shape Rg shape_rg25.41
Total Rg total_rg26.12
Total atoms total_atoms4840
Residues n_residues621
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 dmax85.5
Rg (real space) rg_real26.32
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real7.6350e+07
I(0) uncertainty (real space) i0_real_error1.0830e+06
Rg (reciprocal space) rg_reciprocal26.34
I(0) (reciprocal space) i0_reciprocal76350000.0000
Solution quality estimate total_estimate0.8187
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary84.1
Skewness Skewness skewness0.315
Kurtosis Kurtosis kurtosis-0.383
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23490000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.880; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1leva_
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_idd1levf_
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_id1levA01
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_id1levA02
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_id1levF01
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_id1levF02
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)