3mzl

Sec13/Sec31 edge element, loop deletion mutant

Method: X-RAY DIFFRACTION Dmax: 225.9 Å Quality: GOOD

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

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 A; UniProt 1–297 Chain C; UniProt 1–297 Not recorded Protein transport protein SEC31 × 2 (P38968) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.9;289 K;0.1mM bis-Tris propane, 0.2M sodium citrate, 16% polyethylene glycol 3350, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.80 Å R-free 0.300
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 1–297 Chain G; UniProt 1–297 Not recorded Protein transport protein SEC31 × 2 (P38968) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.9;289 K;0.1mM bis-Tris propane, 0.2M sodium citrate, 16% polyethylene glycol 3350, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.80 Å R-free 0.300

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 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SEC13_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–297; UniProt 1–297 Author chain C; PDBConstruct 1–297; UniProt 1–297 Author chain E; PDBConstruct 1–297; UniProt 1–297 Author chain G; PDBConstruct 1–297; UniProt 1–297

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 B; UniProt 370–473 Chain B; UniProt 508–746 Chain D; UniProt 370–473 Chain D; UniProt 508–746 Fragment:UNP residues 370-746, deletion of residues 474-507 Protein transport protein SEC13 × 2 (Q04491) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.9;289 K;0.1mM bis-Tris propane, 0.2M sodium citrate, 16% polyethylene glycol 3350, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.80 Å R-free 0.300
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 370–473 Chain F; UniProt 508–746 Chain H; UniProt 370–473 Chain H; UniProt 508–746 Fragment:UNP residues 370-746, deletion of residues 474-507 Protein transport protein SEC13 × 2 (Q04491) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.9;289 K;0.1mM bis-Tris propane, 0.2M sodium citrate, 16% polyethylene glycol 3350, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.80 Å R-free 0.300

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 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SEC31_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–106; UniProt 370–473 Author chain B; PDBConstruct 107–345; UniProt 508–746 Author chain D; PDBConstruct 3–106; UniProt 370–473 Author chain D; PDBConstruct 107–345; UniProt 508–746 Author chain F; PDBConstruct 3–106; UniProt 370–473 Author chain F; PDBConstruct 107–345; UniProt 508–746 Author chain H; PDBConstruct 3–106; UniProt 370–473 Author chain H; PDBConstruct 107–345; UniProt 508–746

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 3mzl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3mzl
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3mzl
Deposition date deposition_date2010-05-12
Structure title titleSec13/Sec31 edge element, loop deletion mutant
Keywords keywordsalpha-helical-stack, beta-propeller, 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_guinier86.83
Radius of gyration Rg (electron density) rg_electron88.43
Forward intensity I(0) i01008570000.00
Molecular weight molecular_weight271870.0 kDa
Excluded volume excluded_volume341720 ų
Envelope volume envelope_volume628290 ų
Hydration-shell volume shell_volume70416 ų
Envelope diameter envelope_diameter293.5
Shell Rg shell_rg65.52
Envelope Rg envelope_rg84.50
Shape Rg shape_rg88.49
Total Rg total_rg87.80
Total atoms total_atoms19212
Residues n_residues2432
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 dmax225.9
Rg (real space) rg_real80.66
Rg uncertainty (real space) rg_real_error1.14
I(0) (real space) i0_real9.6350e+08
I(0) uncertainty (real space) i0_real_error1.7640e+07
Rg (reciprocal space) rg_reciprocal81.65
I(0) (reciprocal space) i0_reciprocal993400000.0000
Solution quality estimate total_estimate0.8615
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary75.3
Skewness Skewness skewness0.191
Kurtosis Kurtosis kurtosis-1.013
Angular range angular_range— – 0.0900 −1
Current regularization parameter α current_alpha0.5943
Highest regularization parameter α highest_alpha19240000.0000
Real-space data points n_real_points19
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.924; Stabil: 0.985; Sysdev: 1.000; Positv: 1.000; Valcen: 0.471; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 16 domains

CATH v4.4 (16 domains)

Domain ID domain_id3mzlA01
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_id3mzlB01
Class class2 — Mainly Beta
Architecture architecture20 — Single Sheet
Topology topology25 — N-terminal domain of TfIIb
Homologous superfamily homologous superfamily400
Domain ID domain_id3mzlB02
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology140 — Helix Hairpins
Homologous superfamily homologous superfamily1600
Domain ID domain_id3mzlB03
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily980
Domain ID domain_id3mzlC01
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_id3mzlD01
Class class2 — Mainly Beta
Architecture architecture20 — Single Sheet
Topology topology25 — N-terminal domain of TfIIb
Homologous superfamily homologous superfamily400
Domain ID domain_id3mzlD02
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology140 — Helix Hairpins
Homologous superfamily homologous superfamily1600
Domain ID domain_id3mzlD03
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily980
Domain ID domain_id3mzlE01
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_id3mzlF01
Class class2 — Mainly Beta
Architecture architecture20 — Single Sheet
Topology topology25 — N-terminal domain of TfIIb
Homologous superfamily homologous superfamily400
Domain ID domain_id3mzlF02
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology140 — Helix Hairpins
Homologous superfamily homologous superfamily1600
Domain ID domain_id3mzlF03
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily980
Domain ID domain_id3mzlG01
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_id3mzlH01
Class class2 — Mainly Beta
Architecture architecture20 — Single Sheet
Topology topology25 — N-terminal domain of TfIIb
Homologous superfamily homologous superfamily400
Domain ID domain_id3mzlH02
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology140 — Helix Hairpins
Homologous superfamily homologous superfamily1600
Domain ID domain_id3mzlH03
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily980

8. Citations (1)

9. Files and Curves (10)