8fe7

Crystal structure of human O-GlcNAc transferase (OGT) in complex with an exosite-binding peptide (SMG9) and UDP-GlcNAc

Method: X-RAY DIFFRACTION Dmax: 204.4 Å Quality: GOOD

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 313–1031 Not recorded Nonsense-mediated mRNA decay factor SMG9 × 1 (Q9H0W8) UD1 URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;1.9M Ammonium Sulfate, 0.1M Tris pH 8.5, 1% Xylitol Resolution 2.98 Å R-free 0.217
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 313–1031 Not recorded Nonsense-mediated mRNA decay factor SMG9 × 1 (Q9H0W8) UD1 URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;1.9M Ammonium Sulfate, 0.1M Tris pH 8.5, 1% Xylitol Resolution 2.98 Å R-free 0.217
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 313–1031 Not recorded Nonsense-mediated mRNA decay factor SMG9 × 1 (Q9H0W8) UD1 URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;1.9M Ammonium Sulfate, 0.1M Tris pH 8.5, 1% Xylitol Resolution 2.98 Å R-free 0.217
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 313–1031 Not recorded Nonsense-mediated mRNA decay factor SMG9 × 1 (Q9H0W8) UD1 URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;1.9M Ammonium Sulfate, 0.1M Tris pH 8.5, 1% Xylitol Resolution 2.98 Å R-free 0.217

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 O15294-3
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–723; UniProt 313–1031 Author chain C; PDBConstruct 5–723; UniProt 313–1031 Author chain E; PDBConstruct 5–723; UniProt 313–1031 Author chain G; PDBConstruct 5–723; UniProt 313–1031

Nonsense-mediated mRNA decay factor SMG9

OrganismNot specified

UniProt Q9H0W8

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 140–151 Not recorded UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit × 1 (O15294) UD1 URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;1.9M Ammonium Sulfate, 0.1M Tris pH 8.5, 1% Xylitol Resolution 2.98 Å R-free 0.217
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 140–151 Not recorded UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit × 1 (O15294) UD1 URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;1.9M Ammonium Sulfate, 0.1M Tris pH 8.5, 1% Xylitol Resolution 2.98 Å R-free 0.217
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 140–151 Not recorded UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit × 1 (O15294) UD1 URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;1.9M Ammonium Sulfate, 0.1M Tris pH 8.5, 1% Xylitol Resolution 2.98 Å R-free 0.217
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 140–151 Not recorded UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit × 1 (O15294) UD1 URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;1.9M Ammonium Sulfate, 0.1M Tris pH 8.5, 1% Xylitol Resolution 2.98 Å R-free 0.217

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 SMG9_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–12; UniProt 140–151 Author chain D; PDBConstruct 1–12; UniProt 140–151 Author chain F; PDBConstruct 1–12; UniProt 140–151 Author chain H; PDBConstruct 1–12; UniProt 140–151

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 8fe7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8fe7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8fe7
Deposition date deposition_date2022-12-05
Structure title titleCrystal structure of human O-GlcNAc transferase (OGT) in complex with an exosite-binding peptide (SMG9) and UDP-GlcNAc
Keywords keywordsO-GlcNAc transferase, exosite, protein-protein interaction, complex, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier57.22
Radius of gyration Rg (electron density) rg_electron57.67
Forward intensity I(0) i01528560000.00
Molecular weight molecular_weight324530.0 kDa
Excluded volume excluded_volume405530 ų
Envelope volume envelope_volume568100 ų
Hydration-shell volume shell_volume87853 ų
Envelope diameter envelope_diameter200.4
Shell Rg shell_rg53.27
Envelope Rg envelope_rg56.94
Shape Rg shape_rg57.66
Total Rg total_rg57.55
Total atoms total_atoms22788
Residues n_residues2864
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 dmax204.4
Rg (real space) rg_real57.43
Rg uncertainty (real space) rg_real_error2.62
I(0) (real space) i0_real1.5290e+09
I(0) uncertainty (real space) i0_real_error3.2590e+07
Rg (reciprocal space) rg_reciprocal57.01
I(0) (reciprocal space) i0_reciprocal1528000000.0000
Solution quality estimate total_estimate0.8547
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary68.1
Skewness Skewness skewness0.361
Kurtosis Kurtosis kurtosis-0.483
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha85900000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.807; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.873; Smooth: 0.812

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id8fe7A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily11380
Domain ID domain_id8fe7A02
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_id8fe7A03
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2000 — Glycogen Phosphorylase B;
Domain ID domain_id8fe7C01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily11380
Domain ID domain_id8fe7C02
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_id8fe7C03
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2000 — Glycogen Phosphorylase B;
Domain ID domain_id8fe7E01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily11380
Domain ID domain_id8fe7E02
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_id8fe7E03
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2000 — Glycogen Phosphorylase B;
Domain ID domain_id8fe7G01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily11380
Domain ID domain_id8fe7G02
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_id8fe7G03
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)