SAXSdb — 2hym

▼

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

Soluble IFN alpha/beta receptor

Homo sapiens

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 28–239	Not recorded	Interferon alpha-2 × 1 （P01563）	SOLUTION NMR NMR measurement conditions：pH 8；308 K；Ionic strength (raw mmCIF value) 20 mM deuterated tris buffer；Pressure ambient NMR sample composition：0.3 mM Interferon-alpha2 (D,15N), 90% D2O, 10% H2O, 20 mM deuterated tris buffer, 0.02% NaN3 \| 90% D2O, 10% H2O NMR sample composition：0.3 mM Interferon-alpha2 (D,15N, 13C), 5% D2O, 95% H2O, 20 mM deuterated tris buffer, 0.02% NaN3 \| 5% D2O, 95% H2O NMR sample composition：0.3 mM Interferon-alpha2 (D,15N), 5% D2O, 95% H2O, 20 mM deuterated tris buffer, 0.02% NaN3 \| 5% D2O, 95% H2O	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 2HYM	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2KZ1 Inter-molecular interactions in a 44 kDa interferon-receptor complex detected by asymmetric back-protonation and 2D NOESY Deposited 2010-06-10	Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 28–239（212 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 8；305 K；Ionic strength (raw mmCIF value) 25；Pressure ambient NMR sample composition 0.25 mM [U-99% 2H] Interferon alpha, 0.25 mM [U-99% 2H] Soluble IFN alpha/beta receptor, 25 mM [U-2H] TRIS, 0.02 % sodium azide, 100% D2O \| 100% D2O NMR sample composition 0.25 MM [U-99% 2H, 1H-K,R,L,A,M] INTERFERON ALPHA2, 0.25 MM [U-99% 2H, 1H-H,F,W] SOLUBLE IFN ALPHA/BETA RECEPTOR, 25 mM [U-2H] TRIS, 0.02 % sodium azide, 100% D2O \| 100% D2O NMR sample composition 0.25 MM [U-99% 2H, 1H-L] INTERFERON ALPHA2, 0.25 MM [U-99% 2H, 1H-H,W] SOLUBLE IFN ALPHA/BETA RECEPTOR, 25 mM [U-2H] TRIS, 0.02 % sodium azide, 100% D2O \| 100% D2O NMR sample composition 0.25 MM [15N] INTERFERON ALPHA2, 0.25 MM [1H] SOLUBLE IFN ALPHA/BETA RECEPTOR, 25 mM [U-2H] TRIS, 0.02 % sodium azide, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.25 MM [1H] INTERFERON ALPHA2, 0.25 MM [15N] SOLUBLE IFN ALPHA/BETA RECEPTOR, 25 mM [U-2H] TRIS, 0.02 % sodium azide, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q15467_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–212； UniProt 28–239

Interferon alpha-2

Homo sapiens

UniProt P01563

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 24–188	Not recorded	Soluble IFN alpha/beta receptor × 1 （Q15467）	SOLUTION NMR NMR measurement conditions：pH 8；308 K；Ionic strength (raw mmCIF value) 20 mM deuterated tris buffer；Pressure ambient NMR sample composition：0.3 mM Interferon-alpha2 (D,15N), 90% D2O, 10% H2O, 20 mM deuterated tris buffer, 0.02% NaN3 \| 90% D2O, 10% H2O NMR sample composition：0.3 mM Interferon-alpha2 (D,15N, 13C), 5% D2O, 95% H2O, 20 mM deuterated tris buffer, 0.02% NaN3 \| 5% D2O, 95% H2O NMR sample composition：0.3 mM Interferon-alpha2 (D,15N), 5% D2O, 95% H2O, 20 mM deuterated tris buffer, 0.02% NaN3 \| 5% D2O, 95% H2O	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 2HYM	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1ITF INTERFERON ALPHA-2A, NMR, 24 STRUCTURES Deposited 1997-08-22	Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 24–188（165 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.4；298 K	Resolution not provided
1RH2 RECOMBINANT HUMAN INTERFERON-ALPHA 2B Deposited 1996-11-07	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 24–188（165 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions macroseeding；pH 5.6；PROTEIN WAS CRYSTALLIZED FROM 40MM ZINC ACETATE, 30MM CACODYLATE, PH 5.6; MACRO SEEDING WAS PERFORMED TO GET REASONABLE SIZE CRYSTALS., macroseeding	Resolution 2.90 Å R-free 0.311
1RH2 RECOMBINANT HUMAN INTERFERON-ALPHA 2B Deposited 1996-11-07	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 24–188（165 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions macroseeding；pH 5.6；PROTEIN WAS CRYSTALLIZED FROM 40MM ZINC ACETATE, 30MM CACODYLATE, PH 5.6; MACRO SEEDING WAS PERFORMED TO GET REASONABLE SIZE CRYSTALS., macroseeding	Resolution 2.90 Å R-free 0.311
1RH2 RECOMBINANT HUMAN INTERFERON-ALPHA 2B Deposited 1996-11-07	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 24–188（165 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions macroseeding；pH 5.6；PROTEIN WAS CRYSTALLIZED FROM 40MM ZINC ACETATE, 30MM CACODYLATE, PH 5.6; MACRO SEEDING WAS PERFORMED TO GET REASONABLE SIZE CRYSTALS., macroseeding	Resolution 2.90 Å R-free 0.311
1RH2 RECOMBINANT HUMAN INTERFERON-ALPHA 2B Deposited 1996-11-07	Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 24–188（165 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions macroseeding；pH 5.6；PROTEIN WAS CRYSTALLIZED FROM 40MM ZINC ACETATE, 30MM CACODYLATE, PH 5.6; MACRO SEEDING WAS PERFORMED TO GET REASONABLE SIZE CRYSTALS., macroseeding	Resolution 2.90 Å R-free 0.311
1RH2 RECOMBINANT HUMAN INTERFERON-ALPHA 2B Deposited 1996-11-07	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain E 24–188（165 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions macroseeding；pH 5.6；PROTEIN WAS CRYSTALLIZED FROM 40MM ZINC ACETATE, 30MM CACODYLATE, PH 5.6; MACRO SEEDING WAS PERFORMED TO GET REASONABLE SIZE CRYSTALS., macroseeding	Resolution 2.90 Å R-free 0.311
1RH2 RECOMBINANT HUMAN INTERFERON-ALPHA 2B Deposited 1996-11-07	Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain F 24–188（165 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions macroseeding；pH 5.6；PROTEIN WAS CRYSTALLIZED FROM 40MM ZINC ACETATE, 30MM CACODYLATE, PH 5.6; MACRO SEEDING WAS PERFORMED TO GET REASONABLE SIZE CRYSTALS., macroseeding	Resolution 2.90 Å R-free 0.311
2KZ1 Inter-molecular interactions in a 44 kDa interferon-receptor complex detected by asymmetric back-protonation and 2D NOESY Deposited 2010-06-10	Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 24–188（165 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 8；305 K；Ionic strength (raw mmCIF value) 25；Pressure ambient NMR sample composition 0.25 mM [U-99% 2H] Interferon alpha, 0.25 mM [U-99% 2H] Soluble IFN alpha/beta receptor, 25 mM [U-2H] TRIS, 0.02 % sodium azide, 100% D2O \| 100% D2O NMR sample composition 0.25 MM [U-99% 2H, 1H-K,R,L,A,M] INTERFERON ALPHA2, 0.25 MM [U-99% 2H, 1H-H,F,W] SOLUBLE IFN ALPHA/BETA RECEPTOR, 25 mM [U-2H] TRIS, 0.02 % sodium azide, 100% D2O \| 100% D2O NMR sample composition 0.25 MM [U-99% 2H, 1H-L] INTERFERON ALPHA2, 0.25 MM [U-99% 2H, 1H-H,W] SOLUBLE IFN ALPHA/BETA RECEPTOR, 25 mM [U-2H] TRIS, 0.02 % sodium azide, 100% D2O \| 100% D2O NMR sample composition 0.25 MM [15N] INTERFERON ALPHA2, 0.25 MM [1H] SOLUBLE IFN ALPHA/BETA RECEPTOR, 25 mM [U-2H] TRIS, 0.02 % sodium azide, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.25 MM [1H] INTERFERON ALPHA2, 0.25 MM [15N] SOLUBLE IFN ALPHA/BETA RECEPTOR, 25 mM [U-2H] TRIS, 0.02 % sodium azide, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
2LAG Structure of the 44 kDa complex of interferon-alpha2 with the extracellular part of IFNAR2 obtained by 2D-double difference NOESY Deposited 2011-03-13	Different construct Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 24–188（165 aa） Fragment：Extracellular domain residues 28-237	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 8；305 K；Ionic strength (raw mmCIF value) 25；Pressure ambient NMR sample composition 0.25 mM [U-99% 2H] Interferon alpha/beta receptor 2, 0.25 mM [U-99% 2H] Interferon alpha-2, 100% D2O \| 100% D2O	Resolution not provided
2LMS A single GalNAc residue on Threonine-106 modifies the dynamics and the structure of Interferon alpha-2a around the glycosylation site Deposited 2011-12-12	Different oligomeric state Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 24–188（165 aa）	Not recorded	A2G 2-acetamido-2-deoxy-alpha-D-galactopyranose × 1	SOLUTION NMR NMR measurement conditions pH 3.5；298.15 K；Ionic strength (raw mmCIF value) 25；Pressure ambient NMR sample composition 0.85 mM [U-100% 13C; U-100% 15N] Interferon Alpha-2a (O-glycosylated), 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.87 mM [U-100% 13C; U-100% 15N] Interferon Alpha-2a (O-glycosylated), 100% D2O \| 100% D2O	Resolution not provided
3S9D binary complex between IFNa2 and IFNAR2 Deposited 2011-06-01	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 24–188（165 aa） Fragment：IFNa2 (UNP Residues 24-188)	Mutation：H57A, E58A, Q61A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions 293 K；20% (w/v) PEG 3350, 200 mM NaSCN, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.233
3S9D binary complex between IFNa2 and IFNAR2 Deposited 2011-06-01	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 24–188（165 aa） Fragment：IFNa2 (UNP Residues 24-188)	Mutation：H57A, E58A, Q61A	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions 293 K；20% (w/v) PEG 3350, 200 mM NaSCN, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.233
4YPG Structural Insights Into the Neutralization Properties of a Human Anti-Interferon Monoclonal Antibody Deposited 2015-03-12	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 24–182（159 aa）	Not recorded	NI NICKEL (II) ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；0.01 M NiCl2, 0.1 M Tris HCl	Resolution 3.00 Å R-free 0.272
4YPG Structural Insights Into the Neutralization Properties of a Human Anti-Interferon Monoclonal Antibody Deposited 2015-03-12	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain D 24–182（159 aa）	Not recorded	NI NICKEL (II) ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；0.01 M NiCl2, 0.1 M Tris HCl	Resolution 3.00 Å R-free 0.272
4Z5R Rontalizumab Fab bound to Interferon-a2 Deposited 2015-04-02	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain D 24–188（165 aa）	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；lithium sulfate, PEG3350, 1% dioxane	Resolution 3.00 Å R-free 0.251
4Z5R Rontalizumab Fab bound to Interferon-a2 Deposited 2015-04-02	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 24–188（165 aa）	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；lithium sulfate, PEG3350, 1% dioxane	Resolution 3.00 Å R-free 0.251
4Z5R Rontalizumab Fab bound to Interferon-a2 Deposited 2015-04-02	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 24–188（165 aa）	Not recorded	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；lithium sulfate, PEG3350, 1% dioxane	Resolution 3.00 Å R-free 0.251
4Z5R Rontalizumab Fab bound to Interferon-a2 Deposited 2015-04-02	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain G 24–188（165 aa）	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；lithium sulfate, PEG3350, 1% dioxane	Resolution 3.00 Å R-free 0.251
4Z5R Rontalizumab Fab bound to Interferon-a2 Deposited 2015-04-02	Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain H 24–188（165 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；lithium sulfate, PEG3350, 1% dioxane	Resolution 3.00 Å R-free 0.251
4Z5R Rontalizumab Fab bound to Interferon-a2 Deposited 2015-04-02	Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain I 24–188（165 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；lithium sulfate, PEG3350, 1% dioxane	Resolution 3.00 Å R-free 0.251
4Z5R Rontalizumab Fab bound to Interferon-a2 Deposited 2015-04-02	Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 7 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain X 24–188（165 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；lithium sulfate, PEG3350, 1% dioxane	Resolution 3.00 Å R-free 0.251
4Z5R Rontalizumab Fab bound to Interferon-a2 Deposited 2015-04-02	Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 8 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain N 24–188（165 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；lithium sulfate, PEG3350, 1% dioxane	Resolution 3.00 Å R-free 0.251
9GVL type-I interferons autoantibody pmab15 in complex with Interferon alpha-2 Deposited 2024-09-25	Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 24–188（165 aa）	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；291 K；0.2 M (NH4)2SO4 0.1 M NaAcetate pH 4.6 30 %w/w PEG 2000 MME	Resolution 2.01 Å R-free 0.270
9GVL type-I interferons autoantibody pmab15 in complex with Interferon alpha-2 Deposited 2024-09-25	Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 24–188（165 aa）	Not recorded	GOL GLYCEROL × 1 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；291 K；0.2 M (NH4)2SO4 0.1 M NaAcetate pH 4.6 30 %w/w PEG 2000 MME	Resolution 2.01 Å R-free 0.270
9GVO type-I interferons autoantibodies pmab15 and pmab14 in complex with Interferon alpha-2 Deposited 2024-09-25	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 24–188（165 aa）	Not recorded	GOL GLYCEROL × 6 PO4 PHOSPHATE ION × 2 K POTASSIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；0.1 M Hepes pH 7.5 0.8 M Na2H2PO4 0.8 M KH2PO4	Resolution 1.81 Å R-free 0.215
9GW5 type-I interferon autoantibodies pmab3, pmab19 and pmab14 in complex with Interferon alpha-2 Deposited 2024-09-26	Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 24–188（165 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；0.1 M Hepes pH 7.5 1.9 (NH4)2SO4	Resolution 4.00 Å R-free 0.324

11 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	IFNA2_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–165； UniProt 24–188

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	2hym
Deposition date deposition_date	2006-08-07
Structure title title	NMR based Docking Model of the Complex between the Human Type I Interferon Receptor and Human Interferon alpha-2
Keywords keywords	interferon receptor complex, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method method	SOLUTION NMR

▼

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

Radius of gyration Rg (Guinier) rg_guinier	26.10 Å
Radius of gyration Rg (electron density) rg_electron	25.95 Å
Forward intensity I(0) i0	2551280000.00
Molecular weight molecular_weight	435260.0 kDa
Excluded volume excluded_volume	546530 Å³
Envelope volume envelope_volume	86196 Å³
Hydration-shell volume shell_volume	27913 Å³
Envelope diameter envelope_diameter	101.2 Å
Shell Rg shell_rg	32.76 Å
Envelope Rg envelope_rg	26.84 Å
Shape Rg shape_rg	25.96 Å
Total Rg total_rg	26.04 Å
Total atoms total_atoms	60630
Residues n_residues	3770
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	89.5 Å
Rg (real space) rg_real	26.13 Å
Rg uncertainty (real space) rg_real_error	0.80 Å
I(0) (real space) i0_real	2.5510e+09
I(0) uncertainty (real space) i0_real_error	4.0090e+07
Rg (reciprocal space) rg_reciprocal	26.12 Å
I(0) (reciprocal space) i0_reciprocal	2551000000.0000
Solution quality estimate total_estimate	0.8780
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	32.3 Å
Skewness Skewness skewness	0.309
Kurtosis Kurtosis kurtosis	-0.359
Angular range angular_range	— – 0.3050 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	4372000.0000
Real-space data points n_real_points	62
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.840; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.904; Smooth: 0.990

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Soluble IFN alpha/beta receptor
Molecular weight formula_weight	24323.4 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	60630

SYDSPDYTDESCTFKISLRNFRSILSWELKNHSIVPTHYTLLYTIMSKPEDLKVVKNCANTTRSFCDLTDEWRSTHEAYVTVLEGFSGNTTLFSCSHNFWLAIDMSFEPPEFEIVGFTNHINVMVKFPSIVEEELQFDLSLVIEEQSEGIVKKHKPEIKGNMSGNFTYIIDKLIPNTNYCVSVYLEHSDEQAVIKSPLKCTLLPPGQESEFS

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Interferon alpha-2
Molecular weight formula_weight	19264.1 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

▼

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d2hyma1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.2 — Fibronectin type III
Family Family family	b.1.2.1 — Fibronectin type III

Domain ID domain_id	d2hyma2
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.2 — Fibronectin type III
Family Family family	b.1.2.1 — Fibronectin type III

Domain ID domain_id	d2hymb_
Class class	a — All alpha proteins
Fold Fold fold	a.26 — 4-helical cytokines
Superfamily Superfamily superfamily	a.26.1 — 4-helical cytokines
Family Family family	a.26.1.3 — Interferons/interleukin-10 (IL-10)

CATH v4.4 (3 domains)

Domain ID domain_id	2hymA01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	2hymA02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	2hymB00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily	10 —

▶

8. Citations (1)

▶

fit	/app/data/saxs_computation/hy/2hym/2hym.fit
pddf	/app/data/pr_computation/hy/2hym/2hym.pr.out
profile	/app/data/saxs_computation/hy/2hym/2hym.dat

NMR based Docking Model of the Complex between the Human Type I Interferon Receptor and Human Interferon alpha-2

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

Soluble IFN alpha/beta receptor

State in the Current Structure

Other States of the Same Protein in the Database

Interferon alpha-2

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)