4l41

Human Lactose synthase: A 2:1 complex between human alpha-lactalbumin and human beta1,4-galactosyltransferase

Method: X-RAY DIFFRACTION Dmax: 82.3 Å Quality: GOOD

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 19–142 Chain B; UniProt 19–142 Fragment:UNP residues 19-142 Beta-1,4-galactosyltransferase 1 × 1 (P15291) 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

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.

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 1–124; UniProt 19–142 Author chain B; PDBConstruct 1–124; UniProt 19–142

Beta-1,4-galactosyltransferase 1

Homo sapiens

UniProt P15291

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 126–398 Fragment:UNP residues 126-398 Mutation:R337T, C338T Alpha-lactalbumin × 2 (P00709) 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

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.

18 other PDB entries and 57 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B4GT1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 15–287; UniProt 126–398

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 4l41

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4l41
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4l41
Deposition date deposition_date2013-06-07
Structure title titleHuman Lactose synthase: A 2:1 complex between human alpha-lactalbumin and human beta1,4-galactosyltransferase
Keywords keywordsGT-A fold, lactose synthase, Substrate binding, Golgi, Calcium Binding Protein-Transferase complex; Calcium Binding Protein/Transferase
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.13
Radius of gyration Rg (electron density) rg_electron24.18
Forward intensity I(0) i058337500.00
Molecular weight molecular_weight59482.0 kDa
Excluded volume excluded_volume74408 ų
Envelope volume envelope_volume89079 ų
Hydration-shell volume shell_volume30363 ų
Envelope diameter envelope_diameter84.3
Shell Rg shell_rg31.69
Envelope Rg envelope_rg24.03
Shape Rg shape_rg24.13
Total Rg total_rg25.17
Total atoms total_atoms4172
Residues n_residues518
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

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

Maximum dimension Dmax dmax82.3
Rg (real space) rg_real25.00
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real5.8340e+07
I(0) uncertainty (real space) i0_real_error8.3140e+05
Rg (reciprocal space) rg_reciprocal25.04
I(0) (reciprocal space) i0_reciprocal58340000.0000
Solution quality estimate total_estimate0.8936
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.3
Skewness Skewness skewness0.133
Kurtosis Kurtosis kurtosis-0.528
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9762000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.872; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd4l41a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.2 — Lysozyme-like
Superfamily Superfamily superfamilyd.2.1 — Lysozyme-like
Family Family familyd.2.1.0 — automated matches
Domain ID domain_idd4l41b_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.2 — Lysozyme-like
Superfamily Superfamily superfamilyd.2.1 — Lysozyme-like
Family Family familyd.2.1.0 — automated matches
Domain ID domain_idd4l41c_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.68 — Nucleotide-diphospho-sugar transferases
Superfamily Superfamily superfamilyc.68.1 — Nucleotide-diphospho-sugar transferases
Family Family familyc.68.1.2 — beta 1,4 galactosyltransferase (b4GalT1)

CATH v4.4 (3 domains)

Domain ID domain_id4l41A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily10
Domain ID domain_id4l41B00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily10
Domain ID domain_id4l41C00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology550 — Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
Homologous superfamily homologous superfamily10 — Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

8. Citations (1)

9. Files and Curves (10)