7yeh

Cryo-EM structure of human OGT-OGA complex

Method: ELECTRON MICROSCOPY Dmax: 180.8 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–1046 Chain B; UniProt 1–1046 Not recorded Protein O-GlcNAcase × 2 (O60502) UDP URIDINE-5'-DIPHOSPHATE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.92 Å

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 101 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 1–1046; UniProt 1–1046 Author chain B; PDBConstruct 1–1046; UniProt 1–1046

Protein O-GlcNAcase

Homo sapiens

UniProt O60502

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–916 Chain D; UniProt 1–916 Not recorded UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit × 2 (O15294) UDP URIDINE-5'-DIPHOSPHATE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.92 Å

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.

27 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name OGA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–916; UniProt 1–916 Author chain D; PDBConstruct 1–916; UniProt 1–916

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 7yeh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7yeh
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7yeh
Deposition date deposition_date2022-07-05
Structure title titleCryo-EM structure of human OGT-OGA complex
Keywords keywordsO-GlcNAc transferase, O-GlcNAcase, Complex, Mutual inhibition, TRANSFERASE, TRANSFERASE-HYDROLASE complex; TRANSFERASE/HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier54.73
Radius of gyration Rg (electron density) rg_electron54.70
Forward intensity I(0) i01059570000.00
Molecular weight molecular_weight271790.0 kDa
Excluded volume excluded_volume339960 ų
Envelope volume envelope_volume492640 ų
Hydration-shell volume shell_volume76367 ų
Envelope diameter envelope_diameter177.9
Shell Rg shell_rg56.14
Envelope Rg envelope_rg53.01
Shape Rg shape_rg54.67
Total Rg total_rg54.85
Total atoms total_atoms19122
Residues n_residues2419
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 dmax180.8
Rg (real space) rg_real54.66
Rg uncertainty (real space) rg_real_error1.80
I(0) (real space) i0_real1.0600e+09
I(0) uncertainty (real space) i0_real_error2.3550e+07
Rg (reciprocal space) rg_reciprocal54.75
I(0) (reciprocal space) i0_reciprocal1060000000.0000
Solution quality estimate total_estimate0.8881
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary81.0
Skewness Skewness skewness0.129
Kurtosis Kurtosis kurtosis-0.729
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha62670000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.805

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7yehA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily11380
Domain ID domain_id7yehB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily11380

8. Citations (1)

9. Files and Curves (10)