5cxb

Structure of Ytm1 bound to the C-terminal domain of Erb1 in P21 21 2 space group

Method: X-RAY DIFFRACTION Dmax: 102.6 Å Quality: REASONABLE

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

Ribosome biogenesis protein YTM1

Chaetomium thermophilum

UniProt G0SFB5

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 1–495 Not recorded Ribosome biogenesis protein ERB1 × 1 (G0SCK6) EDO 1,2-ETHANEDIOL × 3 NA SODIUM ION × 1 GOL GLYCEROL × 2 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;294 K;20% PEG 8000, 0.1M Hepes pH 7.5 Resolution 2.10 Å R-free 0.213

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 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0SFB5_CHATD
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 20–514; UniProt 1–495

Ribosome biogenesis protein ERB1

Chaetomium thermophilum

UniProt G0SCK6

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 433–801 Not recorded Ribosome biogenesis protein YTM1 × 1 (G0SFB5) EDO 1,2-ETHANEDIOL × 3 NA SODIUM ION × 1 GOL GLYCEROL × 2 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;294 K;20% PEG 8000, 0.1M Hepes pH 7.5 Resolution 2.10 Å R-free 0.213

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.

13 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0SCK6_CHATD
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–369; UniProt 433–801

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 5cxb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5cxb
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5cxb
Deposition date deposition_date2015-07-28
Structure title titleStructure of Ytm1 bound to the C-terminal domain of Erb1 in P21 21 2 space group
Keywords keywordsribosome assembly, WD40, beta-propeller, ubiquitin-like domain, protein binding; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.27
Radius of gyration Rg (electron density) rg_electron29.76
Forward intensity I(0) i0127459000.00
Molecular weight molecular_weight89203.0 kDa
Excluded volume excluded_volume111610 ų
Envelope volume envelope_volume137000 ų
Hydration-shell volume shell_volume38487 ų
Envelope diameter envelope_diameter107.6
Shell Rg shell_rg36.69
Envelope Rg envelope_rg30.06
Shape Rg shape_rg29.73
Total Rg total_rg30.46
Total atoms total_atoms6295
Residues n_residues817
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 dmax102.6
Rg (real space) rg_real30.29
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real1.2750e+08
I(0) uncertainty (real space) i0_real_error2.2840e+06
Rg (reciprocal space) rg_reciprocal30.29
I(0) (reciprocal space) i0_reciprocal127500000.0000
Solution quality estimate total_estimate0.6892
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.5
Skewness Skewness skewness0.394
Kurtosis Kurtosis kurtosis-0.269
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha28860000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.822; Stabil: 1.000; Sysdev: 0.193; Positv: 1.000; Valcen: 0.977; Smooth: 0.933

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id5cxbA02
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_id5cxbB00
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)