5csm

YEAST CHORISMATE MUTASE, T226S MUTANT, COMPLEX WITH TRP

Method: X-RAY DIFFRACTION Dmax: 67.4 Å Quality: REASONABLE

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

CHORISMATE MUTASE

Saccharomyces cerevisiae

UniProt P32178

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–256 Mutation:T226S TRP TRYPTOPHAN × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;HANGING DROP, 19 % PEG 3350, 3 MM DTT, 0.16 M SODIUM ACETATE PH 5.0, 16 MM TRYPTOPHAN, 10 MG/ML PROTEIN, vapor diffusion - hanging drop Resolution 2.00 Å R-free 0.236

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.

4 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CHMU_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–256; UniProt 1–256

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 5csm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5csm
Deposition date deposition_date1997-07-14
Structure title titleYEAST CHORISMATE MUTASE, T226S MUTANT, COMPLEX WITH TRP
Keywords keywords;CHORISMATE PYRUVATEMUTASE, ALLOSTERIC PROTEIN, COMPLEX (ISOMERASE-PEPTIDE), TRANSITION STATE ANALOG, COMPLEX (ISOMERASE-PEPTIDE) complex ;; COMPLEX (ISOMERASE/PEPTIDE)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.52
Radius of gyration Rg (electron density) rg_electron19.41
Forward intensity I(0) i013864600.00
Molecular weight molecular_weight29246.0 kDa
Excluded volume excluded_volume37213 ų
Envelope volume envelope_volume44041 ų
Hydration-shell volume shell_volume19200 ų
Envelope diameter envelope_diameter66.3
Shell Rg shell_rg25.48
Envelope Rg envelope_rg19.66
Shape Rg shape_rg19.40
Total Rg total_rg20.36
Total atoms total_atoms2066
Residues n_residues250
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 dmax67.4
Rg (real space) rg_real20.43
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real1.3860e+07
I(0) uncertainty (real space) i0_real_error2.0220e+05
Rg (reciprocal space) rg_reciprocal20.45
I(0) (reciprocal space) i0_reciprocal13860000.0000
Solution quality estimate total_estimate0.6406
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary25.4
Skewness Skewness skewness0.190
Kurtosis Kurtosis kurtosis-0.490
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2572000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.866; Stabil: 1.000; Sysdev: 0.242; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd5csma_
Class classa — All alpha proteins
Fold Fold folda.130 — Chorismate mutase II
Superfamily Superfamily superfamilya.130.1 — Chorismate mutase II
Family Family familya.130.1.2 — Allosteric chorismate mutase

CATH v4.4 (1 domains)

Domain ID domain_id5csmA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology590 — Chorismate Mutase, subunit A
Homologous superfamily homologous superfamily10 — Chorismate mutase, AroQ class superfamily, eukaryotic

8. Citations (4)

9. Files and Curves (10)