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1ar2

DISULFIDE-FREE IMMUNOGLOBULIN FRAGMENT

Method: X-RAY DIFFRACTION Dmax: 50.2 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

REI

Homo sapiens

UniProt P01607

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 1–107 Fragment：VARIABLE REGION, LIGHT CHAIN Mutation：INS(TP-1D), C25V, Y34H No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；pH 4.6；277 K；VAPOUR DIFFUSION AL 4 C FROM A PROTEIN SOLUTION CONTAINING 8 MG/ML IN 50 MM POTASSIUM PHOSPHATE BUFFER AL PH 7, USING 2 M AMMONIUM SULFATE IN 100 MM SODIUM ACETATE BUFFER, PH 4.6, vapor diffusion, temperature 277K Resolution 2.80 Å R-free 0.415

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 1AR2 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BWW BENCE-JONES IMMUNOGLOBULIN REI VARIABLE PORTION, T39K MUTANT Deposited 1998-09-29 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–107（107 aa） Fragment：IMMUNOGLOBULIN KAPPA LIGHT CHAIN
Chain B 1–107（107 aa） Fragment：IMMUNOGLOBULIN KAPPA LIGHT CHAIN
Mutation：T39K Mutation：T39K No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；20% PEG 8000, 100 MM HEPES PH7 10 MG/ML PROTEIN IN 50 MM PHOSPHATE PH7, pH 7.0
Resolution 1.70 Å R-free 0.221
1REI THE MOLECULAR STRUCTURE OF A DIMER COMPOSED OF THE VARIABLE PORTIONS OF THE BENCE-JONES PROTEIN REI REFINED AT 2.0 ANGSTROMS RESOLUTION Deposited 1976-03-17 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–107（107 aa）
Chain B 1–107（107 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å
4L1H Bence-Jones immunoglobulin REI variable portion with seven point mutations Deposited 2013-06-03 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–107（107 aa）
Mutation：Q24R,N34A,T39K,Y71F,F73L,I83F,Q105E No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.68 Å R-free 0.260
4L1H Bence-Jones immunoglobulin REI variable portion with seven point mutations Deposited 2013-06-03 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–107（107 aa）
Mutation：Q24R,N34A,T39K,Y71F,F73L,I83F,Q105E No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.68 Å R-free 0.260

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KV1O_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 3–109； UniProt 1–107

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 1ar2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ar2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1ar2
Deposition date deposition_date1997-08-08
Structure title titleDISULFIDE-FREE IMMUNOGLOBULIN FRAGMENT
Keywords keywordsDISULFIDE-FREE, IMMUNOGLOBULIN FRAGMENT, BENCE-JONES, IMMUNOGLOBULIN; IMMUNOGLOBULIN
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier14.45 Å
Radius of gyration Rg (electron density) rg_electron13.36 Å
Forward intensity I(0) i02918600.00
Molecular weight molecular_weight11913.0 kDa
Excluded volume excluded_volume14871 ų
Envelope volume envelope_volume16145 ų
Hydration-shell volume shell_volume10604 ų
Envelope diameter envelope_diameter49.8 Å
Shell Rg shell_rg18.76 Å
Envelope Rg envelope_rg13.72 Å
Shape Rg shape_rg13.31 Å
Total Rg total_rg14.65 Å
Total atoms total_atoms840
Residues n_residues109
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 dmax50.2 Å
Rg (real space) rg_real14.41 Å
Rg uncertainty (real space) rg_real_error0.35 Å
I(0) (real space) i0_real2.9190e+06
I(0) uncertainty (real space) i0_real_error3.3210e+04
Rg (reciprocal space) rg_reciprocal14.42 Å
I(0) (reciprocal space) i0_reciprocal2919000.0000
Solution quality estimate total_estimate0.8598
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.2 Å
Skewness Skewness skewness0.296
Kurtosis Kurtosis kurtosis-0.197
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha615800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.738; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.984
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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_idd1ar2a_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)

CATH v4.4 (1 domains)

Domain ID domain_id1ar2A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
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8. Citations (1)

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9. Files and Curves (10)