5ggp

Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with GlcNAc-beta1,2-Man-peptide

Method: X-RAY DIFFRACTION Dmax: 71.3 Å Quality: REASONABLE

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

Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1

Homo sapiens

UniProt Q8WZA1

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 Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 92–250 Fragment:UNP residues 92-250 10-mer Peptide from Dystroglycan × 1 (Q14118) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose × 1 NA SODIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;MES-NaOH, LiCl2, Na acetate, PEG-6000 Resolution 1.60 Å R-free 0.246
2 Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 92–250 Fragment:UNP residues 92-250 10-mer Peptide from Dystroglycan × 1 (Q14118) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose × 1 NA SODIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;MES-NaOH, LiCl2, Na acetate, PEG-6000 Resolution 1.60 Å R-free 0.246

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.

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

View Construct and Data Evidence
UniProt name PMGT1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–164; UniProt 92–250 Author chain B; PDBConstruct 6–164; UniProt 92–250

10-mer Peptide from Dystroglycan

OrganismNot specified

UniProt Q14118

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 Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 316–325 Not recorded Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1 × 1 (Q8WZA1) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose × 1 NA SODIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;MES-NaOH, LiCl2, Na acetate, PEG-6000 Resolution 1.60 Å R-free 0.246
2 Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 316–325 Not recorded Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1 × 1 (Q8WZA1) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose × 1 NA SODIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;MES-NaOH, LiCl2, Na acetate, PEG-6000 Resolution 1.60 Å R-free 0.246

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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DAG1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–10; UniProt 316–325 Author chain D; PDBConstruct 1–10; UniProt 316–325

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 5ggp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5ggp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5ggp
Deposition date deposition_date2016-06-16
Structure title titleCrystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with GlcNAc-beta1,2-Man-peptide
Keywords keywordsglycosyltransferease, O-mannosylation, alpha-dystroglycan, SUGAR BINDING PROTEIN; SUGAR BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.58
Radius of gyration Rg (electron density) rg_electron20.71
Forward intensity I(0) i019589200.00
Molecular weight molecular_weight34467.0 kDa
Excluded volume excluded_volume43489 ų
Envelope volume envelope_volume50897 ų
Hydration-shell volume shell_volume20712 ų
Envelope diameter envelope_diameter72.4
Shell Rg shell_rg26.88
Envelope Rg envelope_rg20.80
Shape Rg shape_rg20.71
Total Rg total_rg21.54
Total atoms total_atoms2425
Residues n_residues314
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 dmax71.3
Rg (real space) rg_real21.52
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real1.9590e+07
I(0) uncertainty (real space) i0_real_error2.3860e+05
Rg (reciprocal space) rg_reciprocal21.53
I(0) (reciprocal space) i0_reciprocal19590000.0000
Solution quality estimate total_estimate0.7269
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.2
Skewness Skewness skewness0.232
Kurtosis Kurtosis kurtosis-0.519
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4449000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 0.281; Positv: 1.000; Valcen: 0.985; Smooth: 0.975

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)