4rey

Crystal Structure of the GRASP65-GM130 C-terminal peptide complex

Method: X-RAY DIFFRACTION Dmax: 67.1 Å Quality: GOOD

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

Golgi reassembly-stacking protein 1

Homo sapiens

UniProt Q9BQQ3

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 2–210 Fragment:GRASP domain of GRAS65, UNP residues 1-210 Golgin subfamily A member 2 × 1 (Q08379) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;291 K;30% PEG 4000, 0.1M Tris, 0.2M Lithium sulfate, , pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 1.96 Å R-free 0.190

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GORS1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–213; UniProt 2–210

Golgin subfamily A member 2

Homo sapiens

UniProt Q08379

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 980–1002 Fragment:GM130 C-TERMINAL DOMAIN, UNP residues 980-1002 Golgi reassembly-stacking protein 1 × 1 (Q9BQQ3) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;291 K;30% PEG 4000, 0.1M Tris, 0.2M Lithium sulfate, , pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 1.96 Å R-free 0.190

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GOGA2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 5–27; UniProt 980–1002

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 4rey

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4rey
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4rey
Deposition date deposition_date2014-09-24
Structure title titleCrystal Structure of the GRASP65-GM130 C-terminal peptide complex
Keywords keywordsPDZ fold six-stranded anti parallel-barrel capped by two-helices, protein interaction, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.48
Radius of gyration Rg (electron density) rg_electron18.60
Forward intensity I(0) i010933200.00
Molecular weight molecular_weight24190.0 kDa
Excluded volume excluded_volume30133 ų
Envelope volume envelope_volume35799 ų
Hydration-shell volume shell_volume16683 ų
Envelope diameter envelope_diameter68.4
Shell Rg shell_rg24.08
Envelope Rg envelope_rg18.82
Shape Rg shape_rg18.58
Total Rg total_rg19.50
Total atoms total_atoms3355
Residues n_residues218
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 dmax67.1
Rg (real space) rg_real19.49
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real1.0930e+07
I(0) uncertainty (real space) i0_real_error1.4540e+05
Rg (reciprocal space) rg_reciprocal19.49
I(0) (reciprocal space) i0_reciprocal10930000.0000
Solution quality estimate total_estimate0.8599
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.8
Skewness Skewness skewness0.404
Kurtosis Kurtosis kurtosis-0.124
Angular range angular_range— – 0.4100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2063000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.742; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.964; Smooth: 0.987

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_id4reyA01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology42 — Pdz3 Domain
Homologous superfamily homologous superfamily10 — PDZ domain
Domain ID domain_id4reyA02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology42 — Pdz3 Domain
Homologous superfamily homologous superfamily10 — PDZ domain

8. Citations (1)

9. Files and Curves (10)