6hm8

Crystal structure of human ACBD3 GOLD domain in complex with 3A protein of enterovirus-D68 (fusion protein)

Method: X-RAY DIFFRACTION Dmax: 56.3 Å Quality: GOOD

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

Golgi resident protein GCP60

Homo sapiens

UniProt Q9H3P7

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 364–528 Not recorded Genome polyprotein × 1 (A0A2K9Y515) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;10% w/v PEG 8000, 6% v/v 1,5-pentanediol, 14% v/v PEG 200, 10 mM spermine, 10 mM spermidine, 10 mM DL-ornithine, 10 mM 1,4-diaminobutane, 200 mM NaCl, 100 mM GlyGly/AMPD pH 8.5 Resolution 2.28 Å R-free 0.233

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.

11 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCP60_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–168; UniProt 364–528

Genome polyprotein

Enterovirus D68

UniProt A0A2K9Y515

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 1454–1498 Not recorded Golgi resident protein GCP60 × 1 (Q9H3P7) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;10% w/v PEG 8000, 6% v/v 1,5-pentanediol, 14% v/v PEG 200, 10 mM spermine, 10 mM spermidine, 10 mM DL-ornithine, 10 mM 1,4-diaminobutane, 200 mM NaCl, 100 mM GlyGly/AMPD pH 8.5 Resolution 2.28 Å R-free 0.233

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A2K9Y515_9ENTO
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 6–50; UniProt 1454–1498

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 6hm8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6hm8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6hm8
Deposition date deposition_date2018-09-12
Structure title titleCrystal structure of human ACBD3 GOLD domain in complex with 3A protein of enterovirus-D68 (fusion protein)
Keywords keywordscomplex, Golgi, enterovirus, picornavirus, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.81
Radius of gyration Rg (electron density) rg_electron15.65
Forward intensity I(0) i07172700.00
Molecular weight molecular_weight19755.0 kDa
Excluded volume excluded_volume24792 ų
Envelope volume envelope_volume27855 ų
Hydration-shell volume shell_volume14949 ų
Envelope diameter envelope_diameter57.4
Shell Rg shell_rg21.80
Envelope Rg envelope_rg16.11
Shape Rg shape_rg15.62
Total Rg total_rg16.84
Total atoms total_atoms1401
Residues n_residues171
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 dmax56.3
Rg (real space) rg_real16.72
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real7.1730e+06
I(0) uncertainty (real space) i0_real_error9.2680e+04
Rg (reciprocal space) rg_reciprocal16.73
I(0) (reciprocal space) i0_reciprocal7173000.0000
Solution quality estimate total_estimate0.7939
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.9
Skewness Skewness skewness0.204
Kurtosis Kurtosis kurtosis-0.259
Angular range angular_range— – 0.4750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2016000.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.772; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)