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2lms

A single GalNAc residue on Threonine-106 modifies the dynamics and the structure of Interferon alpha-2a around the glycosylation site

Method: SOLUTION NMR Dmax: 45.6 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 24–188 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

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 2LMS 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 ligand/ion 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 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 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 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 ligand/ion 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 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 ligand/ion 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
2HYM NMR based Docking Model of the Complex between the Human Type I Interferon Receptor and Human Interferon alpha-2 Deposited 2006-08-07 Different oligomeric state Different ligand/ion Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 24–188（165 aa）
Not recorded No recorded non-water small molecule 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
2KZ1 Inter-molecular interactions in a 44 kDa interferon-receptor complex detected by asymmetric back-protonation and 2D NOESY Deposited 2010-06-10 Different oligomeric state Different ligand/ion 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 oligomeric state Different ligand/ion 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
3S9D binary complex between IFNa2 and IFNAR2 Deposited 2011-06-01 Different construct Different mutation/modification Different oligomeric state 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） 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 oligomeric state 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 oligomeric state 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 oligomeric state 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 ligand/ion 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 1
Chains and sequence ranges Author chain A； PDBConstruct 2–166； 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.

SAXS scattering curve SAXS Profile

SAXS profile for 2lms

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2lms
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2lms
Deposition date deposition_date2011-12-12
Structure title titleA single GalNAc residue on Threonine-106 modifies the dynamics and the structure of Interferon alpha-2a around the glycosylation site
Keywords keywordsCYTOKINE, GLYCOPROTEIN, O-GLYCOSYLATION, SIGNALING PROTEIN, TYPE I INTERFERONS, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier16.22 Å
Radius of gyration Rg (electron density) rg_electron16.04 Å
Forward intensity I(0) i02022920000.00
Molecular weight molecular_weight388530.0 kDa
Excluded volume excluded_volume488400 ų
Envelope volume envelope_volume40771 ų
Hydration-shell volume shell_volume18897 ų
Envelope diameter envelope_diameter58.8 Å
Shell Rg shell_rg24.41 Å
Envelope Rg envelope_rg18.21 Å
Shape Rg shape_rg15.99 Å
Total Rg total_rg16.36 Å
Total atoms total_atoms54440
Residues n_residues3300
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 dmax45.6 Å
Rg (real space) rg_real16.11 Å
Rg uncertainty (real space) rg_real_error0.18 Å
I(0) (real space) i0_real2.0230e+09
I(0) uncertainty (real space) i0_real_error1.8500e+07
Rg (reciprocal space) rg_reciprocal16.12 Å
I(0) (reciprocal space) i0_reciprocal2023000000.0000
Solution quality estimate total_estimate0.8532
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.1 Å
Skewness Skewness skewness0.104
Kurtosis Kurtosis kurtosis-0.452
Angular range angular_range— – 0.4900 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha639100.0000
Real-space data points n_real_points79
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.962; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.213
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2lmsa_
Class classa — All alpha proteins
Fold Fold folda.26 — 4-helical cytokines
Superfamily Superfamily superfamilya.26.1 — 4-helical cytokines
Family Family familya.26.1.3 — Interferons/interleukin-10 (IL-10)

CATH v4.4 (1 domains)

Domain ID domain_id2lmsA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily10 —
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8. Citations (1)

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9. Files and Curves (10)