4odn

Structure of SlyD from Thermus thermophilus in complex with S2-plus peptide

Method: X-RAY DIFFRACTION Dmax: 67.9 Å Quality: REASONABLE

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

Peptidyl-prolyl cis-trans isomerase SlyD

Thermus thermophilus

UniProt Q5SLE7

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 1–149 Not recorded 30S ribosomal protein S2 × 1 (P0A7V0) SO4 SULFATE ION × 3 GOL GLYCEROL × 2 CL CHLORIDE ION × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;277 K;20% PEG6000, 0.1 M citric acid, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 1.60 Å R-free 0.198

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.

15 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q5SLE7_THET8
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–149; UniProt 1–149

30S ribosomal protein S2

OrganismNot specified

UniProt P0A7V0

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 26–41 Fragment:S2-plus peptide (UNP residues 26-41) Mutation:I41Y Non-standard monomer:Yes (specific site not provided by mmCIF) Peptidyl-prolyl cis-trans isomerase SlyD × 1 (Q5SLE7) SO4 SULFATE ION × 3 GOL GLYCEROL × 2 CL CHLORIDE ION × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;277 K;20% PEG6000, 0.1 M citric acid, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 1.60 Å R-free 0.198

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.

400 other PDB entries and 452 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS2_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–16; UniProt 26–41

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 4odn

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4odn
Deposition date deposition_date2014-01-10
Structure title titleStructure of SlyD from Thermus thermophilus in complex with S2-plus peptide
Keywords keywordsFKBP domain, IF domain, chaperone, peptidyl-prolyl isomerase, PPIase, ISOMERASE; ISOMERASE, CHAPERONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.06
Radius of gyration Rg (electron density) rg_electron20.42
Forward intensity I(0) i06544310.00
Molecular weight molecular_weight18405.0 kDa
Excluded volume excluded_volume22745 ų
Envelope volume envelope_volume29194 ų
Hydration-shell volume shell_volume12798 ų
Envelope diameter envelope_diameter66.9
Shell Rg shell_rg25.11
Envelope Rg envelope_rg20.21
Shape Rg shape_rg20.39
Total Rg total_rg21.23
Total atoms total_atoms1292
Residues n_residues162
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 dmax67.9
Rg (real space) rg_real21.16
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real6.5440e+06
I(0) uncertainty (real space) i0_real_error8.8060e+04
Rg (reciprocal space) rg_reciprocal21.14
I(0) (reciprocal space) i0_reciprocal6544000.0000
Solution quality estimate total_estimate0.7089
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.0
Skewness Skewness skewness0.315
Kurtosis Kurtosis kurtosis-0.747
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1125000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.817; Stabil: 1.000; Sysdev: 0.368; Positv: 1.000; Valcen: 0.768; Smooth: 0.888

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id4odnA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology50 — Chitinase A; domain 3
Homologous superfamily homologous superfamily40

8. Citations (1)

9. Files and Curves (10)