6ej9

Human Xylosyltransferase 1 in complex with peptide QEPEGSGGGQGG

Method: X-RAY DIFFRACTION Dmax: 93.0 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) PO4 PHOSPHATE ION × 2 NA SODIUM ION × 1 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 0.1M of NPS mix (0.033M of each) Resolution 2.02 Å R-free 0.225

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 210–220 Mutation:E212P, L220G, V221G Xylosyltransferase 1 × 1 (Q86Y38) PO4 PHOSPHATE ION × 2 NA SODIUM ION × 1 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 0.1M of NPS mix (0.033M of each) Resolution 2.02 Å R-free 0.225

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 1–11; UniProt 210–220

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 6ej9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ej9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6ej9
Deposition date deposition_date2017-09-20
Structure title titleHuman Xylosyltransferase 1 in complex with peptide QEPEGSGGGQGG
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_guinier29.25
Radius of gyration Rg (electron density) rg_electron28.44
Forward intensity I(0) i0101224000.00
Molecular weight molecular_weight79383.0 kDa
Excluded volume excluded_volume99263 ų
Envelope volume envelope_volume123710 ų
Hydration-shell volume shell_volume35915 ų
Envelope diameter envelope_diameter99.6
Shell Rg shell_rg36.11
Envelope Rg envelope_rg28.41
Shape Rg shape_rg28.41
Total Rg total_rg29.27
Total atoms total_atoms10869
Residues n_residues712
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 dmax93.0
Rg (real space) rg_real29.17
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real1.0120e+08
I(0) uncertainty (real space) i0_real_error1.4860e+06
Rg (reciprocal space) rg_reciprocal29.21
I(0) (reciprocal space) i0_reciprocal101200000.0000
Solution quality estimate total_estimate0.9065
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.4
Skewness Skewness skewness0.227
Kurtosis Kurtosis kurtosis-0.489
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16170000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.932; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.986

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)