1zei

CROSS-LINKED B28 ASP INSULIN

Method: X-RAY DIFFRACTION Dmax: 57.1 Å Quality: GOOD

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

INSULIN

Sus scrofa

UniProt P01315

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–51 Chain B; UniProt 1–51 Chain C; UniProt 1–51 Chain D; UniProt 1–51 Chain E; UniProt 1–51 Chain F; UniProt 1–51 Mutation:P28D CRS M-CRESOL × 8 ZN ZINC ION × 2 CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.4;pH 6.4 Resolution 1.90 Å R-free 0.232

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.

41 other PDB entries and 126 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INS_PIG
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–53; UniProt 1–51 Author chain B; PDBConstruct 1–53; UniProt 1–51 Author chain C; PDBConstruct 1–53; UniProt 1–51 Author chain D; PDBConstruct 1–53; UniProt 1–51 Author chain E; PDBConstruct 1–53; UniProt 1–51 Author chain F; PDBConstruct 1–53; UniProt 1–51

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 1zei

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1zei
Deposition date deposition_date1998-07-14
Structure title titleCROSS-LINKED B28 ASP INSULIN
Keywords keywordsHORMONE, METABOLIC ROLE, CHEMICAL ACTIVITY, INSULIN MUTANT, CROSS-LINK, GLUCOSE METABOLISM, DIABETES; HORMONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.04
Radius of gyration Rg (electron density) rg_electron18.92
Forward intensity I(0) i023966900.00
Molecular weight molecular_weight36952.0 kDa
Excluded volume excluded_volume45882 ų
Envelope volume envelope_volume54767 ų
Hydration-shell volume shell_volume23282 ų
Envelope diameter envelope_diameter60.5
Shell Rg shell_rg26.08
Envelope Rg envelope_rg18.97
Shape Rg shape_rg18.94
Total Rg total_rg19.79
Total atoms total_atoms2570
Residues n_residues318
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 dmax57.1
Rg (real space) rg_real19.86
Rg uncertainty (real space) rg_real_error0.23
I(0) (real space) i0_real2.3970e+07
I(0) uncertainty (real space) i0_real_error2.6570e+05
Rg (reciprocal space) rg_reciprocal19.90
I(0) (reciprocal space) i0_reciprocal23970000.0000
Solution quality estimate total_estimate0.8319
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.9
Skewness Skewness skewness-0.002
Kurtosis Kurtosis kurtosis-0.533
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7729000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.947; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1zeia_
Class classg — Small proteins
Fold Fold foldg.1 — Insulin-like
Superfamily Superfamily superfamilyg.1.1 — Insulin-like
Family Family familyg.1.1.1 — Insulin-like
Domain ID domain_idd1zeib_
Class classg — Small proteins
Fold Fold foldg.1 — Insulin-like
Superfamily Superfamily superfamilyg.1.1 — Insulin-like
Family Family familyg.1.1.1 — Insulin-like
Domain ID domain_idd1zeic_
Class classg — Small proteins
Fold Fold foldg.1 — Insulin-like
Superfamily Superfamily superfamilyg.1.1 — Insulin-like
Family Family familyg.1.1.1 — Insulin-like
Domain ID domain_idd1zeid_
Class classg — Small proteins
Fold Fold foldg.1 — Insulin-like
Superfamily Superfamily superfamilyg.1.1 — Insulin-like
Family Family familyg.1.1.1 — Insulin-like
Domain ID domain_idd1zeie_
Class classg — Small proteins
Fold Fold foldg.1 — Insulin-like
Superfamily Superfamily superfamilyg.1.1 — Insulin-like
Family Family familyg.1.1.1 — Insulin-like
Domain ID domain_idd1zeif_
Class classg — Small proteins
Fold Fold foldg.1 — Insulin-like
Superfamily Superfamily superfamilyg.1.1 — Insulin-like
Family Family familyg.1.1.1 — Insulin-like

CATH v4.4 (6 domains)

Domain ID domain_id1zeiA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology100 — Insulin-like, subunit E
Homologous superfamily homologous superfamily10 — Insulin-like
Domain ID domain_id1zeiB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology100 — Insulin-like, subunit E
Homologous superfamily homologous superfamily10 — Insulin-like
Domain ID domain_id1zeiC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology100 — Insulin-like, subunit E
Homologous superfamily homologous superfamily10 — Insulin-like
Domain ID domain_id1zeiD00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology100 — Insulin-like, subunit E
Homologous superfamily homologous superfamily10 — Insulin-like
Domain ID domain_id1zeiE00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology100 — Insulin-like, subunit E
Homologous superfamily homologous superfamily10 — Insulin-like
Domain ID domain_id1zeiF00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology100 — Insulin-like, subunit E
Homologous superfamily homologous superfamily10 — Insulin-like

8. Citations (3)

9. Files and Curves (10)