2aes

Crystal Structure of Human M340H-Beta1,4-Galactosyltransferase-I (M340H-B4Gal-T1) in Complex with GlcNAc-beta1,2-Man-alpha1,3-Man-beta-OR

Method: X-RAY DIFFRACTION Dmax: 122.0 Å Quality: GOOD

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

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 Other combination Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 125–397 Fragment:Catalytic domain, Residues 126-398 Mutation:M340H, C338T, R337T 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose × 1 MN MANGANESE (II) ION × 1 SO4 SULFATE ION × 4 UDH 6-AMINOHEXYL-URIDINE-C1,5'-DIPHOSPHATE × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;mes, ammonium sulfate, dioxane, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.00 Å R-free 0.232
2 Other combination Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 125–397 Fragment:Catalytic domain, Residues 126-398 Mutation:M340H, C338T, R337T 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose × 1 MN MANGANESE (II) ION × 1 SO4 SULFATE ION × 6 UDH 6-AMINOHEXYL-URIDINE-C1,5'-DIPHOSPHATE × 1 GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;mes, ammonium sulfate, dioxane, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.00 Å R-free 0.232
3 Other combination Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 125–397 Fragment:Catalytic domain, Residues 126-398 Mutation:M340H, C338T, R337T 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose × 1 MN MANGANESE (II) ION × 1 SO4 SULFATE ION × 3 UDH 6-AMINOHEXYL-URIDINE-C1,5'-DIPHOSPHATE × 1 GOL GLYCEROL × 1 DIO 1,4-DIETHYLENE DIOXIDE × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;mes, ammonium sulfate, dioxane, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.00 Å R-free 0.232

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 55 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B4GT1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 15–287; UniProt 125–397 Author chain B; PDBConstruct 15–287; UniProt 125–397 Author chain C; PDBConstruct 15–287; UniProt 125–397

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 2aes

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2aes
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2aes
Deposition date deposition_date2005-07-23
Structure title titleCrystal Structure of Human M340H-Beta1,4-Galactosyltransferase-I (M340H-B4Gal-T1) in Complex with GlcNAc-beta1,2-Man-alpha1,3-Man-beta-OR
Keywords keywordsbeta1, 4-Galactosyltransferase-I; Trisaccharide; 13arm; Closed conformation; Mutant, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier36.24
Radius of gyration Rg (electron density) rg_electron36.32
Forward intensity I(0) i0158589000.00
Molecular weight molecular_weight99576.0 kDa
Excluded volume excluded_volume123540 ų
Envelope volume envelope_volume149780 ų
Hydration-shell volume shell_volume36513 ų
Envelope diameter envelope_diameter129.8
Shell Rg shell_rg39.69
Envelope Rg envelope_rg36.18
Shape Rg shape_rg36.31
Total Rg total_rg36.58
Total atoms total_atoms6977
Residues n_residues816
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 dmax122.0
Rg (real space) rg_real36.54
Rg uncertainty (real space) rg_real_error1.15
I(0) (real space) i0_real1.5860e+08
I(0) uncertainty (real space) i0_real_error2.7440e+06
Rg (reciprocal space) rg_reciprocal36.36
I(0) (reciprocal space) i0_reciprocal158600000.0000
Solution quality estimate total_estimate0.8002
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.7
Skewness Skewness skewness0.459
Kurtosis Kurtosis kurtosis-0.447
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha81630000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.719; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.674; Smooth: 0.569

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2aesa_
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)
Domain ID domain_idd2aesb_
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)
Domain ID domain_idd2aesc_
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_id2aesA00
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
Domain ID domain_id2aesB00
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
Domain ID domain_id2aesC00
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)