1elz

E. COLI ALKALINE PHOSPHATASE MUTANT (S102G)

Method: X-RAY DIFFRACTION Dmax: 99.3 Å Quality: GOOD

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

ALKALINE PHOSPHATASE

Escherichia coli

UniProt P00634

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 23–471 Chain B; UniProt 23–471 Mutation:S102G ZN ZINC ION × 4 MG MAGNESIUM ION × 2 PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;25 MG/ML PROTEIN IN 39% SATURATING (NH4)2SO4, 100 MM TRIS, 10 MM MGCL2 100 MM ZNCL2, 2 MM NAH2PO4 AT PH 7.5, EQUILIBRATED AGAINST 55% SATURATING (NH4)2SO4 Resolution 2.80 Å R-free 0.173

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 67 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PPB_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–449; UniProt 23–471 Author chain B; PDBConstruct 1–449; UniProt 23–471

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 1elz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1elz
Deposition date deposition_date1998-02-10
Structure title titleE. COLI ALKALINE PHOSPHATASE MUTANT (S102G)
Keywords keywordsALKALINE PHOSPHATASE, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.48
Radius of gyration Rg (electron density) rg_electron27.93
Forward intensity I(0) i0153580000.00
Molecular weight molecular_weight94505.0 kDa
Excluded volume excluded_volume116530 ų
Envelope volume envelope_volume134340 ų
Hydration-shell volume shell_volume39492 ų
Envelope diameter envelope_diameter106.1
Shell Rg shell_rg35.91
Envelope Rg envelope_rg28.25
Shape Rg shape_rg27.94
Total Rg total_rg28.55
Total atoms total_atoms6620
Residues n_residues898
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 dmax99.3
Rg (real space) rg_real28.52
Rg uncertainty (real space) rg_real_error0.89
I(0) (real space) i0_real1.5360e+08
I(0) uncertainty (real space) i0_real_error2.2670e+06
Rg (reciprocal space) rg_reciprocal28.51
I(0) (reciprocal space) i0_reciprocal153600000.0000
Solution quality estimate total_estimate0.8419
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.7
Skewness Skewness skewness0.503
Kurtosis Kurtosis kurtosis0.075
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha37100000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.691; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.896

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1elza_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.76 — Alkaline phosphatase-like
Superfamily Superfamily superfamilyc.76.1 — Alkaline phosphatase-like
Family Family familyc.76.1.1 — Alkaline phosphatase
Domain ID domain_idd1elzb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.76 — Alkaline phosphatase-like
Superfamily Superfamily superfamilyc.76.1 — Alkaline phosphatase-like
Family Family familyc.76.1.1 — Alkaline phosphatase

CATH v4.4 (2 domains)

Domain ID domain_id1elzA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology720 — Alkaline Phosphatase, subunit A
Homologous superfamily homologous superfamily10 — Alkaline Phosphatase, subunit A
Domain ID domain_id1elzB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology720 — Alkaline Phosphatase, subunit A
Homologous superfamily homologous superfamily10 — Alkaline Phosphatase, subunit A

8. Citations (2)

9. Files and Curves (10)