5hgv

Structure of an O-GlcNAc transferase point mutant, D554N in complex with peptide

Method: X-RAY DIFFRACTION Dmax: 121.5 Å Quality: EXCELLENT

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

UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

Homo sapiens

UniProt O15294

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 323–1041 Mutation:D554N TYR-PRO-GLY-GLY-SER-THR-PRO-VAL-SER-SER-ALA-ASN-MET-MET × 1 UDP URIDINE-5'-DIPHOSPHATE × 1 SO4 SULFATE ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;1.6 M Lithium Sulfate, 0.1 M Bis Tris Propane pH 7.0 Resolution 2.05 Å R-free 0.237
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 323–1041 Mutation:D554N TYR-PRO-GLY-GLY-SER-THR-PRO-VAL-SER-SER-ALA-ASN-MET-MET × 1 UDP URIDINE-5'-DIPHOSPHATE × 1 SO4 SULFATE ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;1.6 M Lithium Sulfate, 0.1 M Bis Tris Propane pH 7.0 Resolution 2.05 Å R-free 0.237
3 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 323–1041 Mutation:D554N TYR-PRO-GLY-GLY-SER-THR-PRO-VAL-SER-SER-ALA-ASN-MET-MET × 2 UDP URIDINE-5'-DIPHOSPHATE × 2 SO4 SULFATE ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;1.6 M Lithium Sulfate, 0.1 M Bis Tris Propane pH 7.0 Resolution 2.05 Å R-free 0.237
4 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 323–1041 Mutation:D554N TYR-PRO-GLY-GLY-SER-THR-PRO-VAL-SER-SER-ALA-ASN-MET-MET × 2 UDP URIDINE-5'-DIPHOSPHATE × 2 SO4 SULFATE ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;1.6 M Lithium Sulfate, 0.1 M Bis Tris Propane pH 7.0 Resolution 2.05 Å R-free 0.237

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.

43 other PDB entries and 98 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name OGT1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–719; UniProt 323–1041 Author chain C; PDBConstruct 1–719; UniProt 323–1041

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 5hgv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5hgv
Deposition date deposition_date2016-01-08
Structure title titleStructure of an O-GlcNAc transferase point mutant, D554N in complex with peptide
Keywords keywordsPoint mutant, Glycosyltransferase, OGT, TRANSFERASE-PEPTIDE complex; TRANSFERASE/PEPTIDE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.65
Radius of gyration Rg (electron density) rg_electron37.33
Forward intensity I(0) i0383707000.00
Molecular weight molecular_weight158340.0 kDa
Excluded volume excluded_volume197760 ų
Envelope volume envelope_volume251280 ų
Hydration-shell volume shell_volume54864 ų
Envelope diameter envelope_diameter122.3
Shell Rg shell_rg44.23
Envelope Rg envelope_rg37.15
Shape Rg shape_rg37.35
Total Rg total_rg37.68
Total atoms total_atoms11111
Residues n_residues1397
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 dmax121.5
Rg (real space) rg_real37.60
Rg uncertainty (real space) rg_real_error1.08
I(0) (real space) i0_real3.8370e+08
I(0) uncertainty (real space) i0_real_error6.6320e+06
Rg (reciprocal space) rg_reciprocal37.64
I(0) (reciprocal space) i0_reciprocal383700000.0000
Solution quality estimate total_estimate0.9037
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.5
Skewness Skewness skewness0.245
Kurtosis Kurtosis kurtosis-0.620
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha107100000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.929; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.958

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

Domain ID domain_id5hgvA01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily10 — Tetratricopeptide repeat domain
Domain ID domain_id5hgvA02
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily10 — Tetratricopeptide repeat domain
Domain ID domain_id5hgvA03
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily11380
Domain ID domain_id5hgvA04
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology720 — Signal recognition particle alu RNA binding heterodimer, srp9/1
Homologous superfamily homologous superfamily150
Domain ID domain_id5hgvA05
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2000 — Glycogen Phosphorylase B;
Domain ID domain_id5hgvC01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily10 — Tetratricopeptide repeat domain
Domain ID domain_id5hgvC02
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily10 — Tetratricopeptide repeat domain
Domain ID domain_id5hgvC03
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily11380
Domain ID domain_id5hgvC04
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology720 — Signal recognition particle alu RNA binding heterodimer, srp9/1
Homologous superfamily homologous superfamily150
Domain ID domain_id5hgvC05
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2000 — Glycogen Phosphorylase B;

8. Citations (1)

9. Files and Curves (10)