6cct

Fragment of GID4 in complex with a short peptide

Method: X-RAY DIFFRACTION Dmax: 56.1 Å Quality: GOOD

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

Glucose-induced degradation protein 4 homolog

Homo sapiens

UniProt Q8IVV7

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 124–289 Fragment:residues 124-289 Tetrapeptide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;20% PEG3350, 2% Tacsimate pH 7.0 and 0.1M HEPES pH 7.5 Resolution 2.40 Å R-free 0.260

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.

30 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GID4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–167; UniProt 124–289

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 6cct

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6cct
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6cct
Deposition date deposition_date2018-02-07
Structure title titleFragment of GID4 in complex with a short peptide
Keywords keywordsStructural Genomics, Structural Genomics Consortium, SGC, PEPTIDE BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.55
Radius of gyration Rg (electron density) rg_electron15.13
Forward intensity I(0) i05945560.00
Molecular weight molecular_weight17858.0 kDa
Excluded volume excluded_volume22299 ų
Envelope volume envelope_volume25497 ų
Hydration-shell volume shell_volume14169 ų
Envelope diameter envelope_diameter55.1
Shell Rg shell_rg21.13
Envelope Rg envelope_rg15.58
Shape Rg shape_rg15.10
Total Rg total_rg16.35
Total atoms total_atoms1269
Residues n_residues166
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 dmax56.1
Rg (real space) rg_real16.46
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real5.9460e+06
I(0) uncertainty (real space) i0_real_error7.1150e+04
Rg (reciprocal space) rg_reciprocal16.47
I(0) (reciprocal space) i0_reciprocal5946000.0000
Solution quality estimate total_estimate0.8611
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.4
Skewness Skewness skewness0.241
Kurtosis Kurtosis kurtosis-0.168
Angular range angular_range— – 0.4800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1486000.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.736; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.983

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)