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1g26

THE SOLUTION STRUCTURE OF A WELL-FOLDED PEPTIDE BASED ON THE 31-RESIDUE AMINO-TERMINAL SUBDOMAIN OF HUMAN GRANULIN A

Method: SOLUTION NMR Dmax: 36.3 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

GRANULIN A

OrganismNot specified

UniProt P28799

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 281–311 Fragment：N-TERMINAL DOMAIN (RESIDUES 1-31) Mutation：D1V, K3H, S9I, Q20P No other associated polymer SOLUTION NMR NMR measurement conditions：pH 5；288 K；Pressure ambient NMR measurement conditions：pH 5；298 K；Pressure ambient NMR sample composition：0.5 mM HGA 1-31 (D1V, K3H, S9I, Q20P); 20 mM sodium acetate-d3, 10% D2O, 90% H2O | 10% D2O, 90% H2O NMR sample composition：0.5 mM HGA 1-31 (D1V, K3H, S9I, Q20P); 20 mM sodium acetate-d3, 100% D2O | 100% D2O Resolution not provided

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 1G26 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2JYE Human Granulin A Deposited 2007-12-13 Different construct Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 281–337（57 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.8；298 K；Pressure ambient
NMR measurement conditions pH 6.8；288 K；Pressure ambient
NMR sample composition 10 mM sodium phosphate, 150 mM sodium chloride, 0.2 mM EDTA, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 10 mM sodium phosphate, 150 mM sodium chloride, 0.2 mM EDTA, 100% D2O | 100% D2O
Resolution not provided
2JYT Human Granulin C, isomer 1 Deposited 2007-12-19 Different construct Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 364–417（54 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.8；298 K；Pressure ambient
NMR measurement conditions pH 6.8；288 K；Pressure ambient
NMR sample composition 10 mM sodium phosphate, 150 mM sodium chloride, 0.2 mM EDTA, 0.5-1.0 mM HgrnC1, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 10 mM sodium phosphate, 150 mM sodium chloride, 0.2 mM EDTA, 0.5-1.0 mM HgrnC1, 100% D2O | 100% D2O
Resolution not provided
2JYU Human Granulin C, isomer 2 Deposited 2007-12-19 Different construct Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 364–417（54 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.8；298 K；Pressure ambient
NMR measurement conditions pH 6.8；288 K；Pressure ambient
NMR sample composition 10 mM sodium phosphate, 150 mM sodium chloride, 0.2 mM EDTA, 0.5-1.0 mM HgrnC2, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 10 mM sodium phosphate, 150 mM sodium chloride, 0.2 mM EDTA, 0.5-1.0 mM HgrnC2, 100% D2O | 100% D2O
Resolution not provided
2JYV Human Granulin F Deposited 2007-12-19 Different construct Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 123–179（57 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.8；298 K；Pressure ambient
NMR measurement conditions pH 6.8；288 K；Pressure ambient
NMR sample composition 10 mM sodium phosphate, 150 mM sodium chloride, 0.2 mM EDTA, 0.5-1.0 mM [U-100% 15N] HgrnF, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 10 mM sodium phosphate, 150 mM sodium chloride, 0.2 mM EDTA, 0.5-1.0 mM [U-100% 15N] HgrnF, 100% D2O | 100% D2O
Resolution not provided
6NUG hGRNA4-28_3s Deposited 2019-02-01 Different construct Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 284–307（24 aa） Fragment：residues 284-307
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5；290 K；Pressure 1
NMR sample composition 0.5 mM hGRNA4-28_3s, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
8T8R Sortilin-PGRN peptide complex Deposited 2023-06-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 578–593（16 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；20.00 %w/ PEG 3350, 0.20 M Sodium citrate
Resolution 2.87 Å R-free 0.287
8T8S Sortilin-PGRN peptide complex Deposited 2023-06-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 578–593（16 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CL CHLORIDE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7；293 K；0.10 M Tris, 30.00 %w/v PEG 3000, 0.20 M NaCl
Resolution 2.99 Å R-free 0.275
8T8S Sortilin-PGRN peptide complex Deposited 2023-06-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 578–593（16 aa）
Not recorded CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7；293 K；0.10 M Tris, 30.00 %w/v PEG 3000, 0.20 M NaCl
Resolution 2.99 Å R-free 0.275

7 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRN_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–31； UniProt 281–311

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 1g26

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1g26
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1g26
Deposition date deposition_date2000-10-17
Structure title titleTHE SOLUTION STRUCTURE OF A WELL-FOLDED PEPTIDE BASED ON THE 31-RESIDUE AMINO-TERMINAL SUBDOMAIN OF HUMAN GRANULIN A
Keywords keywordsgranulin/epithelin protein repeats, beta-hairpin stack, CYTOKINE; CYTOKINE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier9.40 Å
Radius of gyration Rg (electron density) rg_electron9.66 Å
Forward intensity I(0) i020015100.00
Molecular weight molecular_weight33729.0 kDa
Excluded volume excluded_volume40840 ų
Envelope volume envelope_volume7696 ų
Hydration-shell volume shell_volume6502 ų
Envelope diameter envelope_diameter38.9 Å
Shell Rg shell_rg15.72 Å
Envelope Rg envelope_rg11.44 Å
Shape Rg shape_rg9.70 Å
Total Rg total_rg9.88 Å
Total atoms total_atoms4390
Residues n_residues310
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 dmax36.3 Å
Rg (real space) rg_real10.01 Å
Rg uncertainty (real space) rg_real_error0.11 Å
I(0) (real space) i0_real2.0240e+07
I(0) uncertainty (real space) i0_real_error1.8060e+05
Rg (reciprocal space) rg_reciprocal9.48 Å
I(0) (reciprocal space) i0_reciprocal20020000.0000
Solution quality estimate total_estimate0.6151
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary10.1 Å
Skewness Skewness skewness0.630
Kurtosis Kurtosis kurtosis0.119
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha4.6500
Highest regularization parameter α highest_alpha9572.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.736; Stabil: 0.872; Sysdev: 0.000; Positv: 1.000; Valcen: 0.449; Smooth: 0.757
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1g26a_
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.16 — Granulin repeat
Family Family familyg.3.16.1 — Granulin repeat
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8. Citations (1)

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9. Files and Curves (10)