SAXSdb — 1a4v

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

ALPHA-LACTALBUMIN

OrganismNot specified

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 20–142	Fragment：CALCIUM-BINDING REGION	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

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 1A4V	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1B9O HUMAN ALPHA-LACTALBUMIN, LOW TEMPERATURE FORM Deposited 1999-02-14	Different construct Different ligand/ion 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
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 Deposited 1999-02-26	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 120–130（11 aa）	Mutation：C11A Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 2.8；283 K；Pressure 1	Resolution not provided
1HML ALPHA_LACTALBUMIN POSSESSES A DISTINCT ZINC BINDING SITE Deposited 1994-09-29	Different construct Different ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 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 1–123； UniProt 20–142

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1a4v
Deposition date deposition_date	1998-02-05
Structure title title	ALPHA-LACTALBUMIN
Keywords keywords	LACTOSE SYNTHASE, CALCIUM BINDING, ALPHA-LACTALBUMIN; LACTOSE SYNTHASE
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	15.56 Å
Radius of gyration Rg (electron density) rg_electron	14.32 Å
Forward intensity I(0) i0	3972510.00
Molecular weight molecular_weight	14151.0 kDa
Excluded volume excluded_volume	17714 Å³
Envelope volume envelope_volume	20059 Å³
Hydration-shell volume shell_volume	12089 Å³
Envelope diameter envelope_diameter	54.0 Å
Shell Rg shell_rg	19.85 Å
Envelope Rg envelope_rg	14.77 Å
Shape Rg shape_rg	14.29 Å
Total Rg total_rg	15.54 Å
Total atoms total_atoms	985
Residues n_residues	123
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

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

Maximum dimension Dmax dmax	54.6 Å
Rg (real space) rg_real	15.52 Å
Rg uncertainty (real space) rg_real_error	0.36 Å
I(0) (real space) i0_real	3.9730e+06
I(0) uncertainty (real space) i0_real_error	4.4740e+04
Rg (reciprocal space) rg_reciprocal	15.52 Å
I(0) (reciprocal space) i0_reciprocal	3973000.0000
Solution quality estimate total_estimate	0.7784
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	20.0 Å
Skewness Skewness skewness	0.280
Kurtosis Kurtosis kurtosis	-0.164
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	563100.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.715; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1a4va_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.2 — Lysozyme-like
Superfamily Superfamily superfamily	d.2.1 — Lysozyme-like
Family Family family	d.2.1.2 — C-type lysozyme

CATH v4.4 (1 domains)

Domain ID domain_id	1a4vA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	530 — Lysozyme
Homologous superfamily homologous superfamily	10 —

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8. Citations (5)

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Unit-cell length a length_a	35.470 Å
Unit-cell length b length_b	69.560 Å
Unit-cell length c length_c	45.960 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	1.800 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.2100
R_work r_work	0.2100
R_free r_free	0.2630

Description description	ALPHA-LACTALBUMIN
Molecular weight formula_weight	14093.1 kDa
EC 编号 ec_number	2.4.1.22
Source method src_method	nat
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1091

ALPHA-LACTALBUMIN

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

ALPHA-LACTALBUMIN

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

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (5)

9. Files and Curves (10)

Files (7)

Curves (3)

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	2

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	106

fit	/app/data/saxs_computation/a4/1a4v/1a4v.fit
pddf	/app/data/pr_computation/a4/1a4v/1a4v.pr.out
profile	/app/data/saxs_computation/a4/1a4v/1a4v.dat