5lvv

Human OGT in complex with UDP and fused substrate peptide (Tab1)

Method: X-RAY DIFFRACTION Dmax: 97.0 Å Quality: GOOD

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

;UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit,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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 199–920 Not recorded UDP URIDINE-5'-DIPHOSPHATE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;3.5M sodium formate, 0.1M Tris pH 8.5 Resolution 2.54 Å R-free 0.245

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 O15294-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 28–749; UniProt 199–920

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 5lvv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5lvv
Deposition date deposition_date2016-09-14
Structure title titleHuman OGT in complex with UDP and fused substrate peptide (Tab1)
Keywords keywordsglycosylation, signalling, O-GlcNAc, O-GlcNAc transferase, substrate recognition, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.91
Radius of gyration Rg (electron density) rg_electron27.42
Forward intensity I(0) i0107886000.00
Molecular weight molecular_weight81594.0 kDa
Excluded volume excluded_volume101870 ų
Envelope volume envelope_volume118100 ų
Hydration-shell volume shell_volume35730 ų
Envelope diameter envelope_diameter101.9
Shell Rg shell_rg34.94
Envelope Rg envelope_rg27.67
Shape Rg shape_rg27.42
Total Rg total_rg28.08
Total atoms total_atoms5731
Residues n_residues720
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 dmax97.0
Rg (real space) rg_real27.89
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real1.0790e+08
I(0) uncertainty (real space) i0_real_error1.5750e+06
Rg (reciprocal space) rg_reciprocal27.90
I(0) (reciprocal space) i0_reciprocal107900000.0000
Solution quality estimate total_estimate0.8669
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.3
Skewness Skewness skewness0.380
Kurtosis Kurtosis kurtosis-0.191
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha34680000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.768; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.980

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id5lvvA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily11380
Domain ID domain_id5lvvA02
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_id5lvvA03
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)