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1bww

BENCE-JONES IMMUNOGLOBULIN REI VARIABLE PORTION, T39K MUTANT

Method: X-RAY DIFFRACTION Dmax: 61.1 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (IG KAPPA CHAIN V-I REGION 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 Chain B； UniProt 1–107 Fragment：IMMUNOGLOBULIN KAPPA LIGHT CHAIN Mutation：T39K No other associated polymer 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

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 1BWW Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1AR2 DISULFIDE-FREE IMMUNOGLOBULIN FRAGMENT Deposited 1997-08-08 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：VARIABLE REGION, LIGHT CHAIN
Mutation：INS(TP-1D), C25V, Y34H No recorded non-water small molecule 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
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 Author chain B； 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 1bww

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1bww
Deposition date deposition_date1998-09-29
Structure title titleBENCE-JONES IMMUNOGLOBULIN REI VARIABLE PORTION, T39K MUTANT
Keywords keywordsREIV, STABILIZED IMMUNOGLOBULIN FRAGMENT, BENCE-JONES PROTEIN, IMMUNE SYSTEM; IMMUNE SYSTEM
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_guinier18.55 Å
Radius of gyration Rg (electron density) rg_electron17.46 Å
Forward intensity I(0) i010452500.00
Molecular weight molecular_weight23943.0 kDa
Excluded volume excluded_volume29913 ų
Envelope volume envelope_volume34372 ų
Hydration-shell volume shell_volume16759 ų
Envelope diameter envelope_diameter56.4 Å
Shell Rg shell_rg23.23 Å
Envelope Rg envelope_rg17.53 Å
Shape Rg shape_rg17.41 Å
Total Rg total_rg18.53 Å
Total atoms total_atoms1686
Residues n_residues218
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 dmax61.1 Å
Rg (real space) rg_real18.94 Å
Rg uncertainty (real space) rg_real_error0.15 Å
I(0) (real space) i0_real1.0340e+07
I(0) uncertainty (real space) i0_real_error1.0110e+05
Rg (reciprocal space) rg_reciprocal18.48 Å
I(0) (reciprocal space) i0_reciprocal10450000.0000
Solution quality estimate total_estimate0.6807
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.6 Å
Skewness Skewness skewness0.328
Kurtosis Kurtosis kurtosis-0.219
Angular range angular_range— – 0.4300 Å−1
Current regularization parameter α current_alpha7.2760
Highest regularization parameter α highest_alpha3497000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.897; Stabil: 0.920; Sysdev: 0.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.438
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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) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1bwwa_
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)
Domain ID domain_idd1bwwb_
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 (2 domains)

Domain ID domain_id1bwwA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1bwwB00
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)