2caz

ESCRT-I core

Method: X-RAY DIFFRACTION Dmax: 93.7 Å Quality: GOOD

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

SUPPRESSOR PROTEIN STP22 OF TEMPERATURE-SENSITIVE ALPHA-FACTOR RECEPTOR AND ARGININE PERMEASE

SACCHAROMYCES CEREVISIAE

UniProt P25604

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 305–385 Fragment:RESIDUES 305-385 VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN VPS28 × 1 (Q02767) PROTEIN SRN2 × 1 (Q99176) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;290 K;8-10% PEG 8000, 8-9% ETHYLENE GLYCOL, 0.1 M HEPES (PH 7.0- 8.0), 17 DEG C Resolution 3.60 Å R-free 0.357
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 305–385 Fragment:RESIDUES 305-385 VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN VPS28 × 1 (Q02767) PROTEIN SRN2 × 1 (Q99176) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;290 K;8-10% PEG 8000, 8-9% ETHYLENE GLYCOL, 0.1 M HEPES (PH 7.0- 8.0), 17 DEG C Resolution 3.60 Å R-free 0.357

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.

6 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name STP22_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–82; UniProt 305–385 Author chain D; PDBConstruct 2–82; UniProt 305–385

VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN VPS28

SACCHAROMYCES CEREVISIAE

UniProt Q02767

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–147 Fragment:RESIDUES 1-147 SUPPRESSOR PROTEIN STP22 OF TEMPERATURE-SENSITIVE ALPHA-FACTOR RECEPTOR AND ARGININE PERMEASE × 1 (P25604) PROTEIN SRN2 × 1 (Q99176) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;290 K;8-10% PEG 8000, 8-9% ETHYLENE GLYCOL, 0.1 M HEPES (PH 7.0- 8.0), 17 DEG C Resolution 3.60 Å R-free 0.357
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 1–147 Fragment:RESIDUES 1-147 SUPPRESSOR PROTEIN STP22 OF TEMPERATURE-SENSITIVE ALPHA-FACTOR RECEPTOR AND ARGININE PERMEASE × 1 (P25604) PROTEIN SRN2 × 1 (Q99176) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;290 K;8-10% PEG 8000, 8-9% ETHYLENE GLYCOL, 0.1 M HEPES (PH 7.0- 8.0), 17 DEG C Resolution 3.60 Å R-free 0.357

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.

6 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPS28_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 9–155; UniProt 1–147 Author chain E; PDBConstruct 9–155; UniProt 1–147

PROTEIN SRN2

SACCHAROMYCES CEREVISIAE

UniProt Q99176

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 130–213 Fragment:RESIDUES 130-213 SUPPRESSOR PROTEIN STP22 OF TEMPERATURE-SENSITIVE ALPHA-FACTOR RECEPTOR AND ARGININE PERMEASE × 1 (P25604) VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN VPS28 × 1 (Q02767) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;290 K;8-10% PEG 8000, 8-9% ETHYLENE GLYCOL, 0.1 M HEPES (PH 7.0- 8.0), 17 DEG C Resolution 3.60 Å R-free 0.357
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 130–213 Fragment:RESIDUES 130-213 SUPPRESSOR PROTEIN STP22 OF TEMPERATURE-SENSITIVE ALPHA-FACTOR RECEPTOR AND ARGININE PERMEASE × 1 (P25604) VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN VPS28 × 1 (Q02767) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;290 K;8-10% PEG 8000, 8-9% ETHYLENE GLYCOL, 0.1 M HEPES (PH 7.0- 8.0), 17 DEG C Resolution 3.60 Å R-free 0.357

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 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SRN2_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 2–85; UniProt 130–213 Author chain F; PDBConstruct 2–85; UniProt 130–213

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 2caz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2caz
Deposition date deposition_date2005-12-23
Structure title titleESCRT-I core
Keywords keywords;PROTEIN TRANSPORT, ESCRT, MVB, MULTIVESICULAR BODIES, ENDOSOME, LYSOSOME, PH DOMAIN, PROTEIN SORTING, VESICLE TRAFFICKING, UBIQUITIN, PHOSPHOINOSITIDE, PTDINS3P, VPS23, VPS28, VPS37, VPS36, COILED COIL, UBL CONJUGATION PATHWAY ;; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.74
Radius of gyration Rg (electron density) rg_electron25.09
Forward intensity I(0) i043671800.00
Molecular weight molecular_weight51106.0 kDa
Excluded volume excluded_volume64110 ų
Envelope volume envelope_volume84945 ų
Hydration-shell volume shell_volume28710 ų
Envelope diameter envelope_diameter98.1
Shell Rg shell_rg31.74
Envelope Rg envelope_rg25.48
Shape Rg shape_rg25.07
Total Rg total_rg25.92
Total atoms total_atoms3602
Residues n_residues442
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 dmax93.7
Rg (real space) rg_real25.76
Rg uncertainty (real space) rg_real_error0.83
I(0) (real space) i0_real4.3670e+07
I(0) uncertainty (real space) i0_real_error6.5620e+05
Rg (reciprocal space) rg_reciprocal25.75
I(0) (reciprocal space) i0_reciprocal43670000.0000
Solution quality estimate total_estimate0.8338
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.7
Skewness Skewness skewness0.452
Kurtosis Kurtosis kurtosis0.086
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8662000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.634; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.968; Smooth: 0.965

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 11 domains

SCOP 2.08 (5 domains)

Domain ID domain_idd2caza1
Class classa — All alpha proteins
Fold Fold folda.2 — Long alpha-hairpin
Superfamily Superfamily superfamilya.2.17 — Endosomal sorting complex assembly domain
Family Family familya.2.17.1 — VPS23 C-terminal domain
Domain ID domain_idd2cazb1
Class classa — All alpha proteins
Fold Fold folda.2 — Long alpha-hairpin
Superfamily Superfamily superfamilya.2.17 — Endosomal sorting complex assembly domain
Family Family familya.2.17.2 — VPS28 N-terminal domain
Domain ID domain_idd2cazc1
Class classa — All alpha proteins
Fold Fold folda.2 — Long alpha-hairpin
Superfamily Superfamily superfamilya.2.17 — Endosomal sorting complex assembly domain
Family Family familya.2.17.3 — VPS37 C-terminal domain-like
Domain ID domain_idd2cazd1
Class classa — All alpha proteins
Fold Fold folda.2 — Long alpha-hairpin
Superfamily Superfamily superfamilya.2.17 — Endosomal sorting complex assembly domain
Family Family familya.2.17.1 — VPS23 C-terminal domain
Domain ID domain_idd2caze1
Class classa — All alpha proteins
Fold Fold folda.2 — Long alpha-hairpin
Superfamily Superfamily superfamilya.2.17 — Endosomal sorting complex assembly domain
Family Family familya.2.17.2 — VPS28 N-terminal domain

CATH v4.4 (6 domains)

Domain ID domain_id2cazA00
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology140 — Helix Hairpins
Homologous superfamily homologous superfamily820
Domain ID domain_id2cazB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1440 — de novo design (two linked rop proteins)
Homologous superfamily homologous superfamily200 — Vps28 N-terminal domain
Domain ID domain_id2cazC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily660 — Helix hairpin bin
Domain ID domain_id2cazD00
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology140 — Helix Hairpins
Homologous superfamily homologous superfamily820
Domain ID domain_id2cazE00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1440 — de novo design (two linked rop proteins)
Homologous superfamily homologous superfamily200 — Vps28 N-terminal domain
Domain ID domain_id2cazF00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily660 — Helix hairpin bin

8. Citations (1)

9. Files and Curves (10)