2fy7

Crystal structure of the catalytic domain of the human beta1,4-galactosyltransferase mutant M339H in apo form

Method: X-RAY DIFFRACTION Dmax: 73.8 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 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 125–397 Fragment:catalytic domain, residues 125-397 Mutation:R337T, C338T, M340H PGE TRIETHYLENE GLYCOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 5.6;298 K;50 mM sodium citrate buffer, 6% PEG 4000, pH 5.6, VAPOR DIFFUSION, temperature 298K Resolution 1.70 Å R-free 0.222

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 1
Chains and sequence ranges Author chain A; 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 2fy7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2fy7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2fy7
Deposition date deposition_date2006-02-07
Structure title titleCrystal structure of the catalytic domain of the human beta1,4-galactosyltransferase mutant M339H in apo form
Keywords keywordsM339H mutant, apo enzyme, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.37
Radius of gyration Rg (electron density) rg_electron18.10
Forward intensity I(0) i016473200.00
Molecular weight molecular_weight30996.0 kDa
Excluded volume excluded_volume38926 ų
Envelope volume envelope_volume44054 ų
Hydration-shell volume shell_volume19955 ų
Envelope diameter envelope_diameter74.3
Shell Rg shell_rg24.84
Envelope Rg envelope_rg18.79
Shape Rg shape_rg18.06
Total Rg total_rg19.19
Total atoms total_atoms2187
Residues n_residues268
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 dmax73.8
Rg (real space) rg_real19.29
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real1.6470e+07
I(0) uncertainty (real space) i0_real_error2.3780e+05
Rg (reciprocal space) rg_reciprocal19.30
I(0) (reciprocal space) i0_reciprocal16470000.0000
Solution quality estimate total_estimate0.7984
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.9
Skewness Skewness skewness0.330
Kurtosis Kurtosis kurtosis0.148
Angular range angular_range— – 0.4100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5206000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.487; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.915; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2fy7a1
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_idd2fy7a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2fy7A00
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)