3n7n

Structure of Csm1/Lrs4 complex

Method: X-RAY DIFFRACTION Dmax: 137.0 Å Quality: REASONABLE

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

Monopolin complex subunit CSM1

Saccharomyces cerevisiae

UniProt P25651

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–190 Chain B; UniProt 1–190 Chain C; UniProt 1–190 Chain D; UniProt 1–190 Not recorded Monopolin complex subunit LRS4 × 2 (Q04087) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;0.1 M Tris-HCl pH 8.5, 120 mM MgCl2, 16% PEG 400, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.90 Å R-free 0.355

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.

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

View Construct and Data Evidence
UniProt name CSM1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–190; UniProt 1–190 Author chain B; PDBConstruct 1–190; UniProt 1–190 Author chain C; PDBConstruct 1–190; UniProt 1–190 Author chain D; PDBConstruct 1–190; UniProt 1–190

Monopolin complex subunit LRS4

Saccharomyces cerevisiae

UniProt Q04087

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 1–102 Chain F; UniProt 1–102 Fragment:UNP Residues 1-102, delta 38-44 Monopolin complex subunit CSM1 × 4 (P25651) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;0.1 M Tris-HCl pH 8.5, 120 mM MgCl2, 16% PEG 400, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.90 Å R-free 0.355

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name LRS4_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–95; UniProt 1–102 Author chain F; PDBConstruct 1–95; UniProt 1–102

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 3n7n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3n7n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3n7n
Deposition date deposition_date2010-05-27
Structure title titleStructure of Csm1/Lrs4 complex
Keywords keywordsmeiosis, rDNA, REPLICATION; REPLICATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier50.00
Radius of gyration Rg (electron density) rg_electron49.98
Forward intensity I(0) i086137900.00
Molecular weight molecular_weight77827.0 kDa
Excluded volume excluded_volume98120 ų
Envelope volume envelope_volume178320 ų
Hydration-shell volume shell_volume32092 ų
Envelope diameter envelope_diameter149.7
Shell Rg shell_rg50.67
Envelope Rg envelope_rg46.23
Shape Rg shape_rg50.03
Total Rg total_rg49.83
Total atoms total_atoms5496
Residues n_residues704
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 dmax137.0
Rg (real space) rg_real49.90
Rg uncertainty (real space) rg_real_error1.52
I(0) (real space) i0_real8.6140e+07
I(0) uncertainty (real space) i0_real_error1.7890e+06
Rg (reciprocal space) rg_reciprocal50.00
I(0) (reciprocal space) i0_reciprocal86150000.0000
Solution quality estimate total_estimate0.6995
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary84.0
Skewness Skewness skewness-0.123
Kurtosis Kurtosis kurtosis-1.040
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4521000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.422; Stabil: 0.995; Sysdev: 1.000; Positv: 1.000; Valcen: 0.837; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id3n7nA01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily340
Domain ID domain_id3n7nA02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1150 — Aspartate Aminotransferase, domain 1
Homologous superfamily homologous superfamily80
Domain ID domain_id3n7nB01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily340
Domain ID domain_id3n7nB02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1150 — Aspartate Aminotransferase, domain 1
Homologous superfamily homologous superfamily80
Domain ID domain_id3n7nC01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily340
Domain ID domain_id3n7nC02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1150 — Aspartate Aminotransferase, domain 1
Homologous superfamily homologous superfamily80
Domain ID domain_id3n7nD01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily340
Domain ID domain_id3n7nD02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1150 — Aspartate Aminotransferase, domain 1
Homologous superfamily homologous superfamily80

8. Citations (1)

9. Files and Curves (10)