4odl

Structure of SlyD from Thermus thermophilus in complex with S2 peptide

Method: X-RAY DIFFRACTION Dmax: 151.1 Å Quality: SUSPICIOUS

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–149 Not recorded 30S ribosomal protein S2 × 2 (P0A7V0) CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;277 K;20% PEG3350, 0.1 M Bis-Tris, pH 5.5, 0.2 M ammonium sulfate, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.92 Å R-free 0.224
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–149 Not recorded 30S ribosomal protein S2 × 2 (P0A7V0) CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;277 K;20% PEG3350, 0.1 M Bis-Tris, pH 5.5, 0.2 M ammonium sulfate, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.92 Å R-free 0.224

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 25 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 Author chain B; 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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 20–34 Chain F; UniProt 20–34 Fragment:S2 peptide (UNP residues 20-34) Non-standard monomer:Yes (specific site not provided by mmCIF) Peptidyl-prolyl cis-trans isomerase SlyD × 1 (Q5SLE7) CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;277 K;20% PEG3350, 0.1 M Bis-Tris, pH 5.5, 0.2 M ammonium sulfate, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.92 Å R-free 0.224
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 20–34 Chain E; UniProt 20–34 Fragment:S2 peptide (UNP residues 20-34) Non-standard monomer:Yes (specific site not provided by mmCIF) Peptidyl-prolyl cis-trans isomerase SlyD × 1 (Q5SLE7) CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;277 K;20% PEG3350, 0.1 M Bis-Tris, pH 5.5, 0.2 M ammonium sulfate, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.92 Å R-free 0.224

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 451 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 C; PDBConstruct 1–15; UniProt 20–34 Author chain D; PDBConstruct 1–15; UniProt 20–34 Author chain E; PDBConstruct 1–15; UniProt 20–34 Author chain F; PDBConstruct 1–15; UniProt 20–34

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 4odl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4odl
Deposition date deposition_date2014-01-10
Structure title titleStructure of SlyD from Thermus thermophilus in complex with S2 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_guinier46.15
Radius of gyration Rg (electron density) rg_electron46.22
Forward intensity I(0) i023029100.00
Molecular weight molecular_weight39431.0 kDa
Excluded volume excluded_volume49359 ų
Envelope volume envelope_volume95197 ų
Hydration-shell volume shell_volume17492 ų
Envelope diameter envelope_diameter120.8
Shell Rg shell_rg53.00
Envelope Rg envelope_rg41.20
Shape Rg shape_rg46.22
Total Rg total_rg46.59
Total atoms total_atoms2785
Residues n_residues354
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 dmax151.1
Rg (real space) rg_real46.55
Rg uncertainty (real space) rg_real_error2.18
I(0) (real space) i0_real2.3030e+07
I(0) uncertainty (real space) i0_real_error5.2320e+05
Rg (reciprocal space) rg_reciprocal46.16
I(0) (reciprocal space) i0_reciprocal23020000.0000
Solution quality estimate total_estimate0.3442
Solution quality rating solution_quality SUSPICIOUS a SUSPICIOUS solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary88.9
Skewness Skewness skewness0.008
Kurtosis Kurtosis kurtosis-1.634
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha750500.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.000; Stabil: 1.000; Sysdev: 0.115; Positv: 1.000; Valcen: 0.124; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4odlA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology50 — Chitinase A; domain 3
Homologous superfamily homologous superfamily40
Domain ID domain_id4odlB00
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)