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1hml

ALPHA_LACTALBUMIN POSSESSES A DISTINCT ZINC BINDING SITE

Method: X-RAY DIFFRACTION Dmax: 54.0 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ALPHA-LACTALBUMIN

Homo sapiens

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 1–142 Not recorded CA CALCIUM ION × 1 ZN ZINC ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.70 Å

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 1HML 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 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） 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 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
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 1–142； UniProt 1–142

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.

SAXS scattering curve SAXS Profile

SAXS profile for 1hml

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1hml
Deposition date deposition_date1994-09-29
Structure title titleALPHA_LACTALBUMIN POSSESSES A DISTINCT ZINC BINDING SITE
Keywords keywordsCALCIUM-BINDING PROTEIN; CALCIUM-BINDING PROTEIN
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_guinier15.69 Å
Radius of gyration Rg (electron density) rg_electron14.41 Å
Forward intensity I(0) i04139660.00
Molecular weight molecular_weight14273.0 kDa
Excluded volume excluded_volume17753 ų
Envelope volume envelope_volume20265 ų
Hydration-shell volume shell_volume12157 ų
Envelope diameter envelope_diameter53.4 Å
Shell Rg shell_rg19.97 Å
Envelope Rg envelope_rg14.85 Å
Shape Rg shape_rg14.38 Å
Total Rg total_rg15.62 Å
Total atoms total_atoms990
Residues n_residues123
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 dmax54.0 Å
Rg (real space) rg_real15.66 Å
Rg uncertainty (real space) rg_real_error0.44 Å
I(0) (real space) i0_real4.1400e+06
I(0) uncertainty (real space) i0_real_error5.8690e+04
Rg (reciprocal space) rg_reciprocal15.66 Å
I(0) (reciprocal space) i0_reciprocal4140000.0000
Solution quality estimate total_estimate0.6400
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.8 Å
Skewness Skewness skewness0.316
Kurtosis Kurtosis kurtosis-0.119
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha605600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.744; Stabil: 1.000; Sysdev: 0.368; Positv: 1.000; Valcen: 0.979; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1hmla_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.2 — Lysozyme-like
Superfamily Superfamily superfamilyd.2.1 — Lysozyme-like
Family Family familyd.2.1.2 — C-type lysozyme

CATH v4.4 (1 domains)

Domain ID domain_id1hmlA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily10 —
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8. Citations (3)

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9. Files and Curves (10)