9fnm

Structure of human haptoglobin

Method: X-RAY DIFFRACTION Dmax: 98.7 Å Quality: SUSPICIOUS

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

Isoform 2 of Haptoglobin alpha chain

OrganismNot specified

UniProt P00738

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 19–101 Chain B; UniProt 162–406 Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 4.5;277 K;6% 2-propanol 0.1 M sodium acetate trihydrate 26% PEG MME 550 Resolution 2.52 Å R-free 0.227

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.

14 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HPT_HUMAN
Isoform P00738-2
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–83; UniProt 19–101 Author chain B; PDBConstruct 1–245; UniProt 162–406

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 9fnm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9fnm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9fnm
Deposition date deposition_date2024-06-10
最后修订 last_revision2025-02-12
Structure title titleStructure of human haptoglobin
Keywords keywordsacute phase, hemolysis, hemoglobin binding, reactive oxygen specis, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.70
Radius of gyration Rg (electron density) rg_electron23.34
Forward intensity I(0) i020887900.00
Molecular weight molecular_weight35010.0 kDa
Excluded volume excluded_volume43924 ų
Envelope volume envelope_volume55671 ų
Hydration-shell volume shell_volume21577 ų
Envelope diameter envelope_diameter103.0
Shell Rg shell_rg28.11
Envelope Rg envelope_rg25.07
Shape Rg shape_rg23.35
Total Rg total_rg23.93
Total atoms total_atoms2465
Residues n_residues312
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 dmax98.7
Rg (real space) rg_real24.12
Rg uncertainty (real space) rg_real_error1.20
I(0) (real space) i0_real2.0890e+07
I(0) uncertainty (real space) i0_real_error2.9330e+05
Rg (reciprocal space) rg_reciprocal24.02
I(0) (reciprocal space) i0_reciprocal20890000.0000
Solution quality estimate total_estimate0.4872
Solution quality rating solution_quality SUSPICIOUS a SUSPICIOUS solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.7
Skewness Skewness skewness0.885
Kurtosis Kurtosis kurtosis0.714
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4960000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.208; Stabil: 1.000; Sysdev: 0.154; Positv: 1.000; Valcen: 0.270; Smooth: 0.976

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)