2pm6

Crystal Structure of yeast Sec13/31 edge element of the COPII vesicular coat, native version

Method: X-RAY DIFFRACTION Dmax: 206.9 Å Quality: REASONABLE

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

Protein transport protein SEC31

Saccharomyces cerevisiae

UniProt P38968

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 370–763 Chain C; UniProt 370–763 Fragment:residues 370-763 Protein transport protein SEC13 × 2 (Q04491) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277 K;15% PEG 4000, 10% DMSO, 6% dioxanie, 0.1M Tris-HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.45 Å R-free 0.301

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.

9 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WEB1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–399; UniProt 370–763 Author chain C; PDBConstruct 6–399; UniProt 370–763

Protein transport protein SEC13

Saccharomyces cerevisiae

UniProt Q04491

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 B; UniProt 1–297 Chain D; UniProt 1–297 Not recorded Protein transport protein SEC31 × 2 (P38968) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277 K;15% PEG 4000, 10% DMSO, 6% dioxanie, 0.1M Tris-HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.45 Å R-free 0.301

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.

19 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SEC13_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–297; UniProt 1–297 Author chain D; PDBConstruct 1–297; UniProt 1–297

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 2pm6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2pm6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2pm6
Deposition date deposition_date2007-04-20
Structure title titleCrystal Structure of yeast Sec13/31 edge element of the COPII vesicular coat, native version
Keywords keywordsbeta propeller, alpha solenoid, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier71.39
Radius of gyration Rg (electron density) rg_electron72.94
Forward intensity I(0) i0277427000.00
Molecular weight molecular_weight140560.0 kDa
Excluded volume excluded_volume176530 ų
Envelope volume envelope_volume285580 ų
Hydration-shell volume shell_volume39658 ų
Envelope diameter envelope_diameter227.1
Shell Rg shell_rg49.08
Envelope Rg envelope_rg71.10
Shape Rg shape_rg73.01
Total Rg total_rg72.04
Total atoms total_atoms9934
Residues n_residues1259
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 dmax206.9
Rg (real space) rg_real72.29
Rg uncertainty (real space) rg_real_error2.10
I(0) (real space) i0_real2.7730e+08
I(0) uncertainty (real space) i0_real_error5.9780e+06
Rg (reciprocal space) rg_reciprocal67.59
I(0) (reciprocal space) i0_reciprocal274900000.0000
Solution quality estimate total_estimate0.6163
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary28.2
Skewness Skewness skewness0.451
Kurtosis Kurtosis kurtosis-1.007
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha4508000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.096; Stabil: 0.988; Sysdev: 1.000; Positv: 1.000; Valcen: 0.095; Smooth: 0.657

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id2pm6A00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily1030
Domain ID domain_id2pm6B01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id2pm6C00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily1030
Domain ID domain_id2pm6D01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase

8. Citations (1)

9. Files and Curves (10)