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1cb3

LOCAL INTERACTIONS DRIVE THE FORMATION OF NON-NATIVE STRUCTURE IN THE DENATURED STATE OF HUMAN ALPHA-LACTALBUMIN: A HIGH RESOLUTION STRUCTURAL CHARACTERIZATION OF A PEPTIDE MODEL IN AQUEOUS SOLUTION

Method: SOLUTION NMR Dmax: 15.6 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

LCA

OrganismNot specified

UniProt P00709

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 120–130 Mutation：C11A Non-standard monomer：Yes (specific site not provided by mmCIF) No other associated polymer SOLUTION NMR NMR measurement conditions：pH 2.8；283 K；Pressure 1 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 1CB3 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1A4V ALPHA-LACTALBUMIN Deposited 1998-02-05 Different construct Different mutation/modification 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 20–142（123 aa） Fragment：CALCIUM-BINDING REGION
Not recorded CA CALCIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；pH 7.5
Resolution 1.80 Å R-free 0.263
1B9O HUMAN ALPHA-LACTALBUMIN, LOW TEMPERATURE FORM Deposited 1999-02-14 Different construct Different mutation/modification 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 1–123（123 aa）
Not recorded CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4.2；pH 4.2
Resolution 1.15 Å R-free 0.162
1HML ALPHA_LACTALBUMIN POSSESSES A DISTINCT ZINC BINDING SITE Deposited 1994-09-29 Different construct Different mutation/modification 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 1–142（142 aa）
Not recorded CA CALCIUM ION × 1 ZN ZINC ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.70 Å
3B0I Crystal structure of recombinant human alpha lactalbumin Deposited 2011-06-10 Different construct Different mutation/modification 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 20–142（123 aa）
Not recorded CA CALCIUM ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；2.0M ammonium sulfate, 0.01M CaCl2, 0.1M MES, 28mg/ml protein, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.80 Å R-free 0.256
3B0O Crystal structure of alpha-lactalbumin Deposited 2011-06-10 Different construct Different mutation/modification 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 21–142（122 aa）
Not recorded CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.7；293 K；1.8M ammonium sulphate, 10mM CaCl2, 0.1M Tris-HCl, 40mg/ml protein, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.61 Å R-free 0.193
3B0O Crystal structure of alpha-lactalbumin Deposited 2011-06-10 Different construct Different mutation/modification 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 21–142（122 aa）
Not recorded CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.7；293 K；1.8M ammonium sulphate, 10mM CaCl2, 0.1M Tris-HCl, 40mg/ml protein, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.61 Å R-free 0.193
4L41 Human Lactose synthase: A 2:1 complex between human alpha-lactalbumin and human beta1,4-galactosyltransferase Deposited 2013-06-07 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 × 3 PDB declaration: trimeric
Chain A 19–142（124 aa） Fragment：UNP residues 19-142
Chain B 19–142（124 aa） Fragment：UNP residues 19-142
Not recorded CA CALCIUM ION × 2 SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；100 mM mes buffer pH 7.0, 12% PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.70 Å R-free 0.237

6 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LALBA_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 2–12； UniProt 120–130

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 1cb3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1cb3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1cb3
Deposition date deposition_date1999-02-26
Structure title titleLOCAL INTERACTIONS DRIVE THE FORMATION OF NON-NATIVE STRUCTURE IN THE DENATURED STATE OF HUMAN ALPHA-LACTALBUMIN: A HIGH RESOLUTION STRUCTURAL CHARACTERIZATION OF A PEPTIDE MODEL IN AQUEOUS SOLUTION
Keywords keywordsMOLTEN GLOBULE STATE, PROTEIN FOLDING, NON-NATIVE INTERACTIONS, ALPHA- LACTALBUMIN; MOLTEN GLOBULE STATE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier5.66 Å
Radius of gyration Rg (electron density) rg_electron6.63 Å
Forward intensity I(0) i030731000.00
Molecular weight molecular_weight53704.0 kDa
Excluded volume excluded_volume69928 ų
Envelope volume envelope_volume3945 ų
Hydration-shell volume shell_volume4462 ų
Envelope diameter envelope_diameter28.2 Å
Shell Rg shell_rg13.01 Å
Envelope Rg envelope_rg9.22 Å
Shape Rg shape_rg6.56 Å
Total Rg total_rg7.17 Å
Total atoms total_atoms7720
Residues n_residues440
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 dmax15.6 Å
Rg (real space) rg_real5.30 Å
Rg uncertainty (real space) rg_real_error0.02 Å
I(0) (real space) i0_real2.9640e+07
I(0) uncertainty (real space) i0_real_error1.6510e+05
Rg (reciprocal space) rg_reciprocal5.88 Å
I(0) (reciprocal space) i0_reciprocal30730000.0000
Solution quality estimate total_estimate0.6507
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary4.7 Å
Skewness Skewness skewness0.343
Kurtosis Kurtosis kurtosis-0.723
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha4.4440
Highest regularization parameter α highest_alpha210.7000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.986; Stabil: 0.978; Sysdev: 0.000; Positv: 1.000; Valcen: 0.570; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1cb3a_
Class classj — Peptides
Fold Fold foldj.57 — alpha-lactalbumin peptide model
Superfamily Superfamily superfamilyj.57.1 — alpha-lactalbumin peptide model
Family Family familyj.57.1.1 — alpha-lactalbumin peptide model
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8. Citations (1)

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9. Files and Curves (10)