4qmf

Structure of the Krr1 and Faf1 complex from Saccharomyces cerevisiae

Method: X-RAY DIFFRACTION Dmax: 91.5 Å Quality: REASONABLE

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

KRR1 small subunit processome component

Saccharomyces cerevisiae

UniProt P25586

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 D; UniProt 32–222 Fragment:UNP residues 32-222 Protein FAF1 × 1 (P40546) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;0.2M tri-ammonium citrate, 20% (w/v) PEG 3350, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.80 Å R-free 0.278
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 32–222 Fragment:UNP residues 32-222 Protein FAF1 × 1 (P40546) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;0.2M tri-ammonium citrate, 20% (w/v) PEG 3350, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.80 Å R-free 0.278

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.

20 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KRR1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–191; UniProt 32–222 Author chain D; PDBConstruct 1–191; UniProt 32–222

Protein FAF1

Saccharomyces cerevisiae

UniProt P40546

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 C; UniProt 145–169 Chain C; UniProt 199–220 Fragment:UNP residues 145-169, 199-220 KRR1 small subunit processome component × 1 (P25586) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;0.2M tri-ammonium citrate, 20% (w/v) PEG 3350, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.80 Å R-free 0.278
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 145–169 Chain A; UniProt 199–220 Fragment:UNP residues 145-169, 199-220 KRR1 small subunit processome component × 1 (P25586) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;0.2M tri-ammonium citrate, 20% (w/v) PEG 3350, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.80 Å R-free 0.278

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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FAF1_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 2–26; UniProt 145–169 Author chain A; PDBConstruct 27–48; UniProt 199–220 Author chain C; PDBConstruct 2–26; UniProt 145–169 Author chain C; PDBConstruct 27–48; UniProt 199–220

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 4qmf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4qmf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4qmf
Deposition date deposition_date2014-06-16
Structure title titleStructure of the Krr1 and Faf1 complex from Saccharomyces cerevisiae
Keywords keywordsprotein-protein complex, K-homology domain, ribosome biogenesis, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.98
Radius of gyration Rg (electron density) rg_electron26.10
Forward intensity I(0) i032321600.00
Molecular weight molecular_weight44888.0 kDa
Excluded volume excluded_volume56950 ų
Envelope volume envelope_volume75725 ų
Hydration-shell volume shell_volume25253 ų
Envelope diameter envelope_diameter97.7
Shell Rg shell_rg32.19
Envelope Rg envelope_rg26.19
Shape Rg shape_rg26.12
Total Rg total_rg26.80
Total atoms total_atoms3147
Residues n_residues389
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 dmax91.5
Rg (real space) rg_real27.09
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real3.2320e+07
I(0) uncertainty (real space) i0_real_error4.9180e+05
Rg (reciprocal space) rg_reciprocal27.06
I(0) (reciprocal space) i0_reciprocal32320000.0000
Solution quality estimate total_estimate0.6816
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.6
Skewness Skewness skewness0.459
Kurtosis Kurtosis kurtosis-0.168
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5443000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.812; Stabil: 1.000; Sysdev: 0.199; Positv: 1.000; Valcen: 0.894; Smooth: 0.931

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_id4qmfB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1370 — Ribosomal Protein S8; Chain: A, domain 1
Homologous superfamily homologous superfamily10 — K Homology domain, type 1
Domain ID domain_id4qmfB02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1370 — Ribosomal Protein S8; Chain: A, domain 1
Homologous superfamily homologous superfamily10 — K Homology domain, type 1
Domain ID domain_id4qmfD01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1370 — Ribosomal Protein S8; Chain: A, domain 1
Homologous superfamily homologous superfamily10 — K Homology domain, type 1
Domain ID domain_id4qmfD02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1370 — Ribosomal Protein S8; Chain: A, domain 1
Homologous superfamily homologous superfamily10 — K Homology domain, type 1

8. Citations (1)

9. Files and Curves (10)