2chs

CRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ANALOG

Method: X-RAY DIFFRACTION D_max: 147.1 Å Quality: GOOD

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

CHORISMATE MUTASE

Bacillus subtilis

UniProt P19080

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain D； UniProt 1–127 Chain E； UniProt 1–127 Chain F； UniProt 1–127	Not recorded	No other associated polymer	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 1.90 Å
2	Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain J； UniProt 1–127 Chain K； UniProt 1–127 Chain L； UniProt 1–127	Not recorded	No other associated polymer	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 1.90 Å
3	Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 1–127 Chain B； UniProt 1–127 Chain C； UniProt 1–127	Not recorded	No other associated polymer	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 1.90 Å
4	Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain G； UniProt 1–127 Chain H； UniProt 1–127 Chain I； UniProt 1–127	Not recorded	No other associated polymer	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 1.90 Å

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.

Other PDB	Difference from Current Entry 2CHS	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1COM THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS: STRUCTURE DETERMINATION OF CHORISMATE MUTASE AND ITS COMPLEXES WITH A TRANSITION STATE ANALOG AND PREPHENATE, AND IMPLICATIONS ON THE MECHANISM OF ENZYMATIC REACTION Deposited 1994-04-08	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–127（127 aa） Chain B 1–127（127 aa） Chain C 1–127（127 aa）	Not recorded	PRE PREPHENIC ACID × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å
1COM THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS: STRUCTURE DETERMINATION OF CHORISMATE MUTASE AND ITS COMPLEXES WITH A TRANSITION STATE ANALOG AND PREPHENATE, AND IMPLICATIONS ON THE MECHANISM OF ENZYMATIC REACTION Deposited 1994-04-08	Different ligand/ion Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain J 1–127（127 aa） Chain K 1–127（127 aa） Chain L 1–127（127 aa）	Not recorded	PRE PREPHENIC ACID × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å
1COM THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS: STRUCTURE DETERMINATION OF CHORISMATE MUTASE AND ITS COMPLEXES WITH A TRANSITION STATE ANALOG AND PREPHENATE, AND IMPLICATIONS ON THE MECHANISM OF ENZYMATIC REACTION Deposited 1994-04-08	Different ligand/ion Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain D 1–127（127 aa） Chain E 1–127（127 aa） Chain F 1–127（127 aa）	Not recorded	PRE PREPHENIC ACID × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å
1COM THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS: STRUCTURE DETERMINATION OF CHORISMATE MUTASE AND ITS COMPLEXES WITH A TRANSITION STATE ANALOG AND PREPHENATE, AND IMPLICATIONS ON THE MECHANISM OF ENZYMATIC REACTION Deposited 1994-04-08	Different ligand/ion Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain G 1–127（127 aa） Chain H 1–127（127 aa） Chain I 1–127（127 aa）	Not recorded	PRE PREPHENIC ACID × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å
1DBF CHORISMATE MUTASE FROM BACILLUS SUBTILIS AT 1.30 ANGSTROM Deposited 1999-11-02	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–127（127 aa） Chain B 1–127（127 aa） Chain C 1–127（127 aa）	Not recorded	SO4 SULFATE ION × 9 GOL GLYCEROL × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 3；298 K；PROTEIN DROP: 5 MICROLITERS PROTEIN SOLUTION, 5 MICROLITERS RESERVOIR. PROTEIN SOLUTION: 13 MG/ML PROTEIN, 100 MM PMSF, 100 MM NACL, 50 MM TRIS PH 7.5, 1 MM EDTA, 1 MM DTT. RESERVOIR SOLUTION: 2.2 M AMMONIUM SULFATE, 100 MM SODIUM ACETATE PH 3.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.30 Å R-free 0.235
1FNJ CRYSTAL STRUCTURE ANALYSIS OF CHORISMATE MUTASE MUTANT C88S/R90K Deposited 2000-08-22	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–127（127 aa）	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；Protein solution: 10 mM Tris-HCl, 2mM DTT, 0.125 mM EDTA, Reservoir solution: 30% PEG 400, 50 mM Tris-HCl, 50 mM Magnesium Chloride, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.90 Å R-free 0.221
1FNK CRYSTAL STRUCTURE ANALYSIS OF CHORISMATE MUTASE MUTANT C88K/R90S Deposited 2000-08-22	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–127（127 aa）	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；Protein solution: 10 mM Tris-HCl, 2mM DTT, 0.125 mM EDTA, Reservoir solution: 30% PEG 400, 50 mM Tris-HCl, 50 mM magnesium chloride, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.00 Å R-free 0.251
2CHT CRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ANALOG Deposited 1994-04-08	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–127（127 aa） Chain B 1–127（127 aa） Chain C 1–127（127 aa）	Not recorded	TSA 8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC ACID × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å
2CHT CRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ANALOG Deposited 1994-04-08	Different ligand/ion Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain D 1–127（127 aa） Chain E 1–127（127 aa） Chain F 1–127（127 aa）	Not recorded	TSA 8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC ACID × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å
2CHT CRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ANALOG Deposited 1994-04-08	Different ligand/ion Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain G 1–127（127 aa） Chain H 1–127（127 aa） Chain I 1–127（127 aa）	Not recorded	TSA 8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC ACID × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å
2CHT CRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ANALOG Deposited 1994-04-08	Different ligand/ion Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain J 1–127（127 aa） Chain K 1–127（127 aa） Chain L 1–127（127 aa）	Not recorded	TSA 8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC ACID × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å
3ZO8 Wild-type chorismate mutase of Bacillus subtilis at 1.6 A resolution Deposited 2013-02-20	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain D 1–127（127 aa） Chain E 1–127（127 aa） Chain F 1–127（127 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；100 MM MMT BUFFER ---MALIC ACID, MES, TRIS, IN MOLAR RATIOS OF 1:2:2, RESPECTIVELY--- PH 6.0, 100 MM MAGNESIUM CHLORIDE, 25% W/V PEG 1000	Resolution 1.59 Å R-free 0.170
3ZO8 Wild-type chorismate mutase of Bacillus subtilis at 1.6 A resolution Deposited 2013-02-20	Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–127（127 aa） Chain B 1–127（127 aa） Chain C 1–127（127 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；100 MM MMT BUFFER ---MALIC ACID, MES, TRIS, IN MOLAR RATIOS OF 1:2:2, RESPECTIVELY--- PH 6.0, 100 MM MAGNESIUM CHLORIDE, 25% W/V PEG 1000	Resolution 1.59 Å R-free 0.170
3ZOP Arg90Cit chorismate mutase of Bacillus subtilis at 1.6 A resolution Deposited 2013-02-22	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–127（127 aa） Chain B 1–127（127 aa） Chain C 1–127（127 aa）	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；100 MM MMT BUFFER ---MALIC ACID, MES, TRIS, IN MOLAR RATIOS OF 1:2:2, RESPECTIVELY--- PH 6.0, 150 MM CALCIUM CHLORIDE, 25% W/V PEG 1000	Resolution 1.61 Å R-free 0.221
3ZOP Arg90Cit chorismate mutase of Bacillus subtilis at 1.6 A resolution Deposited 2013-02-22	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain D 1–127（127 aa） Chain E 1–127（127 aa） Chain F 1–127（127 aa）	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；100 MM MMT BUFFER ---MALIC ACID, MES, TRIS, IN MOLAR RATIOS OF 1:2:2, RESPECTIVELY--- PH 6.0, 150 MM CALCIUM CHLORIDE, 25% W/V PEG 1000	Resolution 1.61 Å R-free 0.221
3ZP4 Arg90Cit chorismate mutase of Bacillus subtilis in complex with a transition state analog Deposited 2013-02-26	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–127（127 aa） Chain B 1–127（127 aa） Chain C 1–127（127 aa）	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	TSA 8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；100 MM MMT BUFFER - MALIC ACID, MES, TRIS, IN MOLAR RATIOS OF 1:2:2, RESPECTIVELY - PH 6.0, 125 MM CALCIUM CHLORIDE, 24% W/V PEG 1000	Resolution 1.80 Å R-free 0.231
3ZP4 Arg90Cit chorismate mutase of Bacillus subtilis in complex with a transition state analog Deposited 2013-02-26	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain D 1–127（127 aa） Chain E 1–127（127 aa） Chain F 1–127（127 aa）	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	TSA 8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；100 MM MMT BUFFER - MALIC ACID, MES, TRIS, IN MOLAR RATIOS OF 1:2:2, RESPECTIVELY - PH 6.0, 125 MM CALCIUM CHLORIDE, 24% W/V PEG 1000	Resolution 1.80 Å R-free 0.231
3ZP7 Arg90Cit chorismate mutase of Bacillus subtilis in complex with chorismate and prephenate Deposited 2013-02-26	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain D 1–127（127 aa） Chain E 1–127（127 aa） Chain F 1–127（127 aa）	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	PRE PREPHENIC ACID × 2 ISJ (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；100 MM MMT BUFFER ---MALIC ACID, MES, TRIS, IN MOLAR RATIOS OF 1:2:2, RESPECTIVELY--- PH 6.0, 125 MM CALCIUM CHLORIDE, 25% W/V PEG 1000	Resolution 1.70 Å R-free 0.218
3ZP7 Arg90Cit chorismate mutase of Bacillus subtilis in complex with chorismate and prephenate Deposited 2013-02-26	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–127（127 aa） Chain B 1–127（127 aa） Chain C 1–127（127 aa）	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	PRE PREPHENIC ACID × 3 ISJ (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；100 MM MMT BUFFER ---MALIC ACID, MES, TRIS, IN MOLAR RATIOS OF 1:2:2, RESPECTIVELY--- PH 6.0, 125 MM CALCIUM CHLORIDE, 25% W/V PEG 1000	Resolution 1.70 Å R-free 0.218

9 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CHMU_BACSU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–127； UniProt 1–127 Author chain B； PDBConstruct 1–127； UniProt 1–127 Author chain C； PDBConstruct 1–127； UniProt 1–127 Author chain D； PDBConstruct 1–127； UniProt 1–127 Author chain E； PDBConstruct 1–127； UniProt 1–127 Author chain F； PDBConstruct 1–127； UniProt 1–127 Author chain G； PDBConstruct 1–127； UniProt 1–127 Author chain H； PDBConstruct 1–127； UniProt 1–127 Author chain I； PDBConstruct 1–127； UniProt 1–127 Author chain J； PDBConstruct 1–127； UniProt 1–127 Author chain K； PDBConstruct 1–127； UniProt 1–127 Author chain L； PDBConstruct 1–127； UniProt 1–127

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2chs
Deposition date deposition_date	1994-04-08
Structure title title	CRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ANALOG
Keywords keywords	ISOMERASE; ISOMERASE
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	43.59 Å
Radius of gyration Rg (electron density) rg_electron	43.45 Å
Forward intensity I(0) i0	354626000.00
Molecular weight molecular_weight	155630.0 kDa
Excluded volume excluded_volume	195850 Å³
Envelope volume envelope_volume	269250 Å³
Hydration-shell volume shell_volume	52964 Å³
Envelope diameter envelope_diameter	152.1 Å
Shell Rg shell_rg	47.04 Å
Envelope Rg envelope_rg	42.11 Å
Shape Rg shape_rg	43.46 Å
Total Rg total_rg	43.57 Å
Total atoms total_atoms	13272
Residues n_residues	1368
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	147.1 Å
Rg (real space) rg_real	43.67 Å
Rg uncertainty (real space) rg_real_error	1.36 Å
I(0) (real space) i0_real	3.5460e+08
I(0) uncertainty (real space) i0_real_error	6.6550e+06
Rg (reciprocal space) rg_reciprocal	43.59 Å
I(0) (reciprocal space) i0_reciprocal	354600000.0000
Solution quality estimate total_estimate	0.8284
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	61.3 Å
Skewness Skewness skewness	0.316
Kurtosis Kurtosis kurtosis	-0.313
Angular range angular_range	— – 0.1800 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	164100000.0000
Real-space data points n_real_points	37
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.695; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.939; Smooth: 0.742

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (12 domains)

Domain ID domain_id	d2chsa_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.79 — Bacillus chorismate mutase-like
Superfamily Superfamily superfamily	d.79.1 — YjgF-like
Family Family family	d.79.1.2 — Chorismate mutase

Domain ID domain_id	d2chsb_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.79 — Bacillus chorismate mutase-like
Superfamily Superfamily superfamily	d.79.1 — YjgF-like
Family Family family	d.79.1.2 — Chorismate mutase

Domain ID domain_id	d2chsc_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.79 — Bacillus chorismate mutase-like
Superfamily Superfamily superfamily	d.79.1 — YjgF-like
Family Family family	d.79.1.2 — Chorismate mutase

Domain ID domain_id	d2chsd_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.79 — Bacillus chorismate mutase-like
Superfamily Superfamily superfamily	d.79.1 — YjgF-like
Family Family family	d.79.1.2 — Chorismate mutase

Domain ID domain_id	d2chse_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.79 — Bacillus chorismate mutase-like
Superfamily Superfamily superfamily	d.79.1 — YjgF-like
Family Family family	d.79.1.2 — Chorismate mutase

Domain ID domain_id	d2chsf_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.79 — Bacillus chorismate mutase-like
Superfamily Superfamily superfamily	d.79.1 — YjgF-like
Family Family family	d.79.1.2 — Chorismate mutase

Domain ID domain_id	d2chsg_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.79 — Bacillus chorismate mutase-like
Superfamily Superfamily superfamily	d.79.1 — YjgF-like
Family Family family	d.79.1.2 — Chorismate mutase

Domain ID domain_id	d2chsh_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.79 — Bacillus chorismate mutase-like
Superfamily Superfamily superfamily	d.79.1 — YjgF-like
Family Family family	d.79.1.2 — Chorismate mutase

Domain ID domain_id	d2chsi_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.79 — Bacillus chorismate mutase-like
Superfamily Superfamily superfamily	d.79.1 — YjgF-like
Family Family family	d.79.1.2 — Chorismate mutase

Domain ID domain_id	d2chsj_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.79 — Bacillus chorismate mutase-like
Superfamily Superfamily superfamily	d.79.1 — YjgF-like
Family Family family	d.79.1.2 — Chorismate mutase

Domain ID domain_id	d2chsk_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.79 — Bacillus chorismate mutase-like
Superfamily Superfamily superfamily	d.79.1 — YjgF-like
Family Family family	d.79.1.2 — Chorismate mutase

Domain ID domain_id	d2chsl_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.79 — Bacillus chorismate mutase-like
Superfamily Superfamily superfamily	d.79.1 — YjgF-like
Family Family family	d.79.1.2 — Chorismate mutase

CATH v4.4 (12 domains)

Domain ID domain_id	2chsA00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	40 — RutC-like

Domain ID domain_id	2chsB00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	40 — RutC-like

Domain ID domain_id	2chsC00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	40 — RutC-like

Domain ID domain_id	2chsD00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	40 — RutC-like

Domain ID domain_id	2chsE00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	40 — RutC-like

Domain ID domain_id	2chsF00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	40 — RutC-like

Domain ID domain_id	2chsG00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	40 — RutC-like

Domain ID domain_id	2chsH00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	40 — RutC-like

Domain ID domain_id	2chsI00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	40 — RutC-like

Domain ID domain_id	2chsJ00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	40 — RutC-like

Domain ID domain_id	2chsK00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	40 — RutC-like

Domain ID domain_id	2chsL00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily	40 — RutC-like

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8. Citations (1)

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Unit-cell length a length_a	102.400 Å
Unit-cell length b length_b	68.300 Å
Unit-cell length c length_c	102.800 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	105.60 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	24

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	0.1940
R_work r_work	0.1940
R_free r_free	—

Description description	CHORISMATE MUTASE
Molecular weight formula_weight	14507.9 kDa
EC 编号 ec_number	5.4.99.5
Source method src_method	man
Copy count entity_count	12

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K,L
Atom count atom_count	14838

CRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ANALOG

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

CHORISMATE MUTASE

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (12 domains)

CATH v4.4 (12 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Bacillus subtilis
NCBI Class编号 ncbi_taxonomy_id	1423

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	522

fit	/app/data/saxs_computation/ch/2chs/2chs.fit
pddf	/app/data/pr_computation/ch/2chs/2chs.pr.out
profile	/app/data/saxs_computation/ch/2chs/2chs.dat