6ej7

Human Xylosyltransferase 1 in complex with UDP-xylose and peptide QEEEGAGGGQGG

Method: X-RAY DIFFRACTION Dmax: 94.1 Å Quality: EXCELLENT

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

Xylosyltransferase 1

Homo sapiens

UniProt Q86Y38

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 232–959 Not recorded Protein AMBP × 1 (P02760) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 UDX URIDINE-5'-DIPHOSPHATE-XYLOPYRANOSE × 1 NA SODIUM ION × 1 PO4 PHOSPHATE ION × 9 EDO 1,2-ETHANEDIOL × 4 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;55-65% Morpheus precipitant mix 2 (PEG8000 and ethylene glycol), 0.1M Bicine/Tris buffer at pH 7.5 0.1 M of Morpheus NPS mix. Resolution 2.00 Å R-free 0.230

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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name XYLT1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 24–751; UniProt 232–959

Protein AMBP

OrganismNot specified

UniProt P02760

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 210–221 Mutation:S215A, L220G, V221G Xylosyltransferase 1 × 1 (Q86Y38) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 UDX URIDINE-5'-DIPHOSPHATE-XYLOPYRANOSE × 1 NA SODIUM ION × 1 PO4 PHOSPHATE ION × 9 EDO 1,2-ETHANEDIOL × 4 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;55-65% Morpheus precipitant mix 2 (PEG8000 and ethylene glycol), 0.1M Bicine/Tris buffer at pH 7.5 0.1 M of Morpheus NPS mix. Resolution 2.00 Å R-free 0.230

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.

10 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AMBP_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–12; UniProt 210–221

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 6ej7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ej7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6ej7
Deposition date deposition_date2017-09-20
Structure title titleHuman Xylosyltransferase 1 in complex with UDP-xylose and peptide QEEEGAGGGQGG
Keywords keywordsProteoglycan, Glycosyltransferase, Golgi, Xylosyltransferase, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.45
Radius of gyration Rg (electron density) rg_electron28.65
Forward intensity I(0) i0115430000.00
Molecular weight molecular_weight82965.0 kDa
Excluded volume excluded_volume102930 ų
Envelope volume envelope_volume129340 ų
Hydration-shell volume shell_volume37045 ų
Envelope diameter envelope_diameter102.2
Shell Rg shell_rg36.54
Envelope Rg envelope_rg28.74
Shape Rg shape_rg28.63
Total Rg total_rg29.46
Total atoms total_atoms11390
Residues n_residues716
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 dmax94.1
Rg (real space) rg_real29.36
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real1.1540e+08
I(0) uncertainty (real space) i0_real_error1.6550e+06
Rg (reciprocal space) rg_reciprocal29.40
I(0) (reciprocal space) i0_reciprocal115400000.0000
Solution quality estimate total_estimate0.9031
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.9
Skewness Skewness skewness0.234
Kurtosis Kurtosis kurtosis-0.479
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17530000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.921; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.973

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)