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1dm3

ACETYLATED BIOSYNTHETIC THIOLASE FROM ZOOGLOEA RAMIGERA IN COMPLEX WITH ACETYL-COA

Method: X-RAY DIFFRACTION Dmax: 121.0 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

BIOSYNTHETIC THIOLASE ACETYLATED AT CYS89

Zoogloea ramigera

UniProt P07097

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 × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain A； UniProt 5–392 Chain B； UniProt 5–392 Chain C； UniProt 5–392 Chain D； UniProt 5–392 Fragment：ENTIRE THIOLASE, ACETYLATED AT CYS89 Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 6 ACO ACETYL COENZYME *A × 4 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5；294 K；0.9 M Ammonium sulfate, 1 M lithium sulfate, 0,1 M sodium acetate, 1 mM DTT, 1mM EDTA, 1mM sodium azide, pH 5, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 2.00 Å R-free 0.256

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 1DM3 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1DLU UNLIGANDED BIOSYNTHETIC THIOLASE FROM ZOOGLOEA RAMIGERA Deposited 1999-12-12 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 4–391（388 aa）
Chain B 4–391（388 aa）
Chain C 4–391（388 aa）
Chain D 4–391（388 aa）
Not recorded SO4 SULFATE ION × 6 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；294 K；AMMONIUM SULPHATE, LITHIUM SULPHATE, SODIUM ACETATE, pH 5, VAPOR DIFFUSION, HANGING DROP, temperature 294K
Resolution 2.25 Å R-free 0.263
1DLV BIOSYNTHETIC THIOLASE FROM ZOOGLOEA RAMIGERA IN COMPLEX WITH COA Deposited 1999-12-12 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 4–391（388 aa）
Chain B 4–391（388 aa）
Chain C 4–391（388 aa）
Chain D 4–391（388 aa）
Not recorded SO4 SULFATE ION × 6 COA COENZYME A × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；294 K；AMMONIUM SULPHATE, LITHIUM SULPHATE, SODIUM ACETATE, pH 5, VAPOR DIFFUSION, HANGING DROP, temperature 294K
Resolution 2.29 Å R-free 0.293
1M1O Crystal structure of biosynthetic thiolase, C89A mutant, complexed with acetoacetyl-CoA Deposited 2002-06-20 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–391（391 aa）
Chain B 1–391（391 aa）
Chain C 1–391（391 aa）
Chain D 1–391（391 aa）
Mutation：C89A Mutation：C89A Mutation：C89A Mutation：C89A SO4 SULFATE ION × 4 CAA ACETOACETYL-COENZYME A × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；295 K；lithium sulphate, ammonium sulphate, pH 5.0, VAPOR DIFFUSION, SITTING DROP at 295K
Resolution 1.95 Å R-free 0.258
1M1T Biosynthetic thiolase, Q64A mutant Deposited 2002-06-20 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–391（391 aa）
Chain B 1–391（391 aa）
Chain C 1–391（391 aa）
Chain D 1–391（391 aa）
Mutation：Q64A Mutation：Q64A Mutation：Q64A Mutation：Q64A SO4 SULFATE ION × 4 GOL GLYCEROL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；295 K；lithium sulphate, ammonium sulphate, pH 6.0, VAPOR DIFFUSION, SITTING DROP at 295K, VAPOR DIFFUSION, HANGING DROP
Resolution 1.94 Å R-free 0.245
1M3K biosynthetic thiolase, inactive C89A mutant Deposited 2002-06-28 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–391（391 aa）
Chain B 1–391（391 aa）
Chain C 1–391（391 aa）
Chain D 1–391（391 aa）
Mutation：C89A Mutation：C89A Mutation：C89A Mutation：C89A SO4 SULFATE ION × 4 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；295 K；lithium sulphate, ammonium sulphate, pH 5.0, VAPOR DIFFUSION, SITTING DROP at 295K
Resolution 1.70 Å R-free 0.243
1M3Z Biosynthetic thiolase, C89A mutant, complexed with acetyl coenzyme A Deposited 2002-07-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–391（391 aa）
Chain B 1–391（391 aa）
Chain C 1–391（391 aa）
Chain D 1–391（391 aa）
Mutation：C89A Mutation：C89A Mutation：C89A Mutation：C89A SO4 SULFATE ION × 4 ACO ACETYL COENZYME *A × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；293 K；lithium sulphate, ammonium sulphate, pH 5.0, VAPOR DIFFUSION, SITTING DROP at 293K
Resolution 1.87 Å R-free 0.242
1M4S Biosynthetic thiolase, Cys89 acetylated, unliganded form Deposited 2002-07-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–391（391 aa）
Chain B 1–391（391 aa）
Chain C 1–391（391 aa）
Chain D 1–391（391 aa）
Mutation：C89 acetylated Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C89 acetylated Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C89 acetylated Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：C89 acetylated Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 4 GOL GLYCEROL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；293 K；lithium sulphate, ammonium sulphate, pH 5.0, VAPOR DIFFUSION, SITTING DROP at 293K
Resolution 1.87 Å R-free 0.247
1M4T Biosynthetic thiolase, Cys89 butyrylated Deposited 2002-07-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–391（391 aa）
Chain B 1–391（391 aa）
Chain C 1–391（391 aa）
Chain D 1–391（391 aa）
Mutation：Cys89 butyrylated Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Cys89 butyrylated Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Cys89 butyrylated Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Cys89 butyrylated Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 4 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；293 K；lithium sulphate, ammonium sulphate, pH 5.0, VAPOR DIFFUSION, SITTING DROP at 293K, VAPOR DIFFUSION, HANGING DROP
Resolution 1.77 Å R-free 0.242
1NL7 Z. ramigera biosynthetic thiolase, acetylated enzyme complexed with CoA at pH 9.5 Deposited 2003-01-06 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–391（391 aa）
Chain B 1–391（391 aa）
Chain C 1–391（391 aa）
Chain D 1–391（391 aa）
Mutation：Cys89 acetylated Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Cys89 acetylated Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Cys89 acetylated Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Cys89 acetylated Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 4 COA COENZYME A × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；295 K；lithium sulphate, ammonium sulphate, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K
Resolution 1.90 Å R-free 0.223
1OU6 Biosynthetic thiolase from Zoogloea ramigera in complex with acetyl-O-pantetheine-11-pivalate Deposited 2003-03-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–391（391 aa）
Chain B 1–391（391 aa）
Chain C 1–391（391 aa）
Chain D 1–391（391 aa）
Mutation：Cys89 hydroxylated Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Cys89 hydroxylated Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Cys89 hydroxylated Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Cys89 hydroxylated Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 4 168 PANTOTHENYL-AMINOETHANOL-ACETATE PIVALIC ACID × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；288 K；ammonium sulfate, lithium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 288K
Resolution 2.07 Å R-free 0.212
1QFL BIOSYNTHETIC THIOLASE FROM ZOOGLOEA RAMIGERA IN COMPLEX WITH A REACTION INTERMEDIATE. Deposited 1999-04-12 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 4–391（388 aa） Fragment：RESIDUES 4-392
Chain B 4–391（388 aa） Fragment：RESIDUES 4-392
Chain C 4–391（388 aa） Fragment：RESIDUES 4-392
Chain D 4–391（388 aa） Fragment：RESIDUES 4-392
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 6 COA COENZYME A × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5；1 M LITHIUM SULPHATE, 0.9 M AMMONIUM SULPHATE, 0.1 M SODIUM ACETATE PH 5.0 A REACTION INTERMEDIATE WAS TRAPPED BY FLASH-FREEZING THE CRYSTAL AFTER A SHORT SOAK WITH ACETOACETYL-COA SUBSTRATE.
Resolution 1.92 Å R-free 0.256
2VTZ Biosynthetic thiolase from Z. ramigera. Complex of the C89A mutant with coenzyme A. Deposited 2008-05-19 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–11（10 aa） Fragment：RESIDUES 2-392
Chain A 12–392（381 aa） Fragment：RESIDUES 2-392
Chain B 2–11（10 aa） Fragment：RESIDUES 2-392
Chain B 12–392（381 aa） Fragment：RESIDUES 2-392
Chain C 2–11（10 aa） Fragment：RESIDUES 2-392
Chain C 12–392（381 aa） Fragment：RESIDUES 2-392
Chain D 2–11（10 aa） Fragment：RESIDUES 2-392
Chain D 12–392（381 aa） Fragment：RESIDUES 2-392
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES COA COENZYME A × 4 SO4 SULFATE ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5；pH 5
Resolution 2.30 Å R-free 0.262
2VU0 Biosynthetic thiolase from Z. ramigera. Complex of the oxidised enzyme with coenzyme A. Deposited 2008-05-19 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–392（391 aa） Fragment：RESIDUES 2-392
Chain B 2–392（391 aa） Fragment：RESIDUES 2-392
Chain C 2–392（391 aa） Fragment：RESIDUES 2-392
Chain D 2–392（391 aa） Fragment：RESIDUES 2-392
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) COA COENZYME A × 2 GOL GLYCEROL × 1 SO4 SULFATE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5；pH 5
Resolution 1.87 Å R-free 0.229
2VU1 Biosynthetic thiolase from Z. ramigera. Complex of with O-pantheteine- 11-pivalate. Deposited 2008-05-19 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–11（10 aa） Fragment：RESIDUES 2-392
Chain A 12–392（381 aa） Fragment：RESIDUES 2-392
Chain B 2–11（10 aa） Fragment：RESIDUES 2-392
Chain B 12–392（381 aa） Fragment：RESIDUES 2-392
Chain C 2–11（10 aa） Fragment：RESIDUES 2-392
Chain C 12–392（381 aa） Fragment：RESIDUES 2-392
Chain D 2–11（10 aa） Fragment：RESIDUES 2-392
Chain D 12–392（381 aa） Fragment：RESIDUES 2-392
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) OPI PANTOTHENYL-AMINOETHANOL-11-PIVALIC ACID × 2 NA SODIUM ION × 1 SO4 SULFATE ION × 5 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5；pH 5
Resolution 1.51 Å R-free 0.247
2VU2 Biosynthetic thiolase from Z. ramigera. Complex with S-pantetheine-11- pivalate. Deposited 2008-05-19 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–11（10 aa） Fragment：RESIDUES 2-392
Chain A 12–392（381 aa） Fragment：RESIDUES 2-392
Chain B 2–11（10 aa） Fragment：RESIDUES 2-392
Chain B 12–392（381 aa） Fragment：RESIDUES 2-392
Chain C 2–11（10 aa） Fragment：RESIDUES 2-392
Chain C 12–392（381 aa） Fragment：RESIDUES 2-392
Chain D 2–11（10 aa） Fragment：RESIDUES 2-392
Chain D 12–392（381 aa） Fragment：RESIDUES 2-392
Not recorded PN5 (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate × 2 SO4 SULFATE ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5；pH 5
Resolution 2.65 Å R-free 0.286
2WKT BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. COMPLEX OF THE N316A MUTANT WITH COENZYME A. Deposited 2009-06-18 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–11（10 aa） Fragment：RESIDUES 2-11,12-392
Chain A 12–392（381 aa） Fragment：RESIDUES 2-11,12-392
Chain B 2–11（10 aa） Fragment：RESIDUES 2-11,12-392
Chain B 12–392（381 aa） Fragment：RESIDUES 2-11,12-392
Chain C 2–11（10 aa） Fragment：RESIDUES 2-11,12-392
Chain C 12–392（381 aa） Fragment：RESIDUES 2-11,12-392
Chain D 2–11（10 aa） Fragment：RESIDUES 2-11,12-392
Chain D 12–392（381 aa） Fragment：RESIDUES 2-11,12-392
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) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Mutation：YES Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 9 K POTASSIUM ION × 1 CL CHLORIDE ION × 1 COA COENZYME A × 4 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；1.9 M (NH4)2SO4, 0.1 M SODIUM CITRATE (PH 6.5), 1 MM EDTA, 1 MM NAN3, 1 MM DTT.
Resolution 2.00 Å R-free 0.236
2WKU BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. THE N316H MUTANT. Deposited 2009-06-18 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–11（10 aa） Fragment：RESIDUES 2-11,12-392
Chain A 12–392（381 aa） Fragment：RESIDUES 2-11,12-392
Chain B 2–11（10 aa） Fragment：RESIDUES 2-11,12-392
Chain B 12–392（381 aa） Fragment：RESIDUES 2-11,12-392
Chain C 2–11（10 aa） Fragment：RESIDUES 2-11,12-392
Chain C 12–392（381 aa） Fragment：RESIDUES 2-11,12-392
Chain D 2–11（10 aa） Fragment：RESIDUES 2-11,12-392
Chain D 12–392（381 aa） Fragment：RESIDUES 2-11,12-392
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES SO4 SULFATE ION × 9 DNO D-mannose × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.5；0.95 M LI2SO4, 1.3 (NH4)2SO4, 0.1 M SODIUM CITRATE (PH 5.5), 1 MM EDTA, 1 MM NAN, 1 MM DTT
Resolution 2.30 Å R-free 0.258
2WKV BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. COMPLEX OF THE N316D MUTANT WITH COENZYME A. Deposited 2009-06-18 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–11（10 aa） Fragment：2-11,12-292
Chain A 12–392（381 aa） Fragment：2-11,12-292
Chain B 2–11（10 aa） Fragment：2-11,12-292
Chain B 12–392（381 aa） Fragment：2-11,12-292
Chain C 2–11（10 aa） Fragment：2-11,12-292
Chain C 12–392（381 aa） Fragment：2-11,12-292
Chain D 2–11（10 aa） Fragment：2-11,12-292
Chain D 12–392（381 aa） Fragment：2-11,12-292
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES SO4 SULFATE ION × 10 NA SODIUM ION × 2 COA COENZYME A × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.7；1.9 M (NH4)2SO4, 0.1 M MES (PH 5.7), 1 MM EDTA, 1 MM NAN3 AND 1 MM DTT
Resolution 2.50 Å R-free 0.238
2WL4 BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. COMPLEX OF THE H348A MUTANT WITH COENZYME A. Deposited 2009-06-22 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–11（10 aa） Fragment：RESIDUES 2-11,12-392
Chain A 12–392（381 aa） Fragment：RESIDUES 2-11,12-392
Chain B 2–11（10 aa） Fragment：RESIDUES 2-11,12-392
Chain B 12–392（381 aa） Fragment：RESIDUES 2-11,12-392
Chain C 2–11（10 aa） Fragment：RESIDUES 2-11,12-392
Chain C 12–392（381 aa） Fragment：RESIDUES 2-11,12-392
Chain D 2–11（10 aa） Fragment：RESIDUES 2-11,12-392
Chain D 12–392（381 aa） Fragment：RESIDUES 2-11,12-392
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) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Mutation：YES Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 25 COA COENZYME A × 2 CL CHLORIDE ION × 3 NA SODIUM ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.5；0.95 M LI2SO4, 1.2 M (NH4)2SO4, 0.1 M SODIUM CITRATE (PH 5.5), 1 MM EDTA, 1 MM NAN3 AND 1 MM DTT
Resolution 1.80 Å R-free 0.270
2WL5 BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. COMPLEX OF THE H348N MUTANT WITH COENZYME A. Deposited 2009-06-22 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–11（10 aa） Fragment：RESIDUES 2-11,12-392
Chain A 12–392（381 aa） Fragment：RESIDUES 2-11,12-392
Chain B 2–11（10 aa） Fragment：RESIDUES 2-11,12-392
Chain B 12–392（381 aa） Fragment：RESIDUES 2-11,12-392
Chain C 2–11（10 aa） Fragment：RESIDUES 2-11,12-392
Chain C 12–392（381 aa） Fragment：RESIDUES 2-11,12-392
Chain D 2–11（10 aa） Fragment：RESIDUES 2-11,12-392
Chain D 12–392（381 aa） Fragment：RESIDUES 2-11,12-392
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) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 14 DNO D-mannose × 4 COA COENZYME A × 2 NA SODIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.5；0.75 M LI2SO4, 1.7 M (NH4)2SO4, 0.1 M SODIUM CITRATE (PH 5.5), 1 MM EDTA, 1 MM NAN3 AND 1 MM DTT
Resolution 1.80 Å R-free 0.257
2WL6 BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. THE N316H-H348N MUTANT. Deposited 2009-06-22 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–11（10 aa） Fragment：RESIDUES 2-11,12-392
Chain A 12–392（381 aa） Fragment：RESIDUES 2-11,12-392
Chain B 2–11（10 aa） Fragment：RESIDUES 2-11,12-392
Chain B 12–392（381 aa） Fragment：RESIDUES 2-11,12-392
Chain C 2–11（10 aa） Fragment：RESIDUES 2-11,12-392
Chain C 12–392（381 aa） Fragment：RESIDUES 2-11,12-392
Chain D 2–11（10 aa） Fragment：RESIDUES 2-11,12-392
Chain D 12–392（381 aa） Fragment：RESIDUES 2-11,12-392
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；0.167 M SODIUM CITRATE (PH 6.5), 1.58 M (NH4)2SO4, 1 MM EDTA, 1 MM NAN3 AND 1 MM DTT
Resolution 2.98 Å R-free 0.291
7LBZ Zoogloea ramigera biosynthetic thiolase Y218E mutant Deposited 2021-01-09 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–392（391 aa）
Chain B 2–392（391 aa）
Chain C 2–392（391 aa）
Chain D 2–392（391 aa）
Mutation：Y218E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y218E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y218E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y218E Non-standard monomer：Yes (specific site not provided by mmCIF) COA COENZYME A × 4 SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；289 K；1 M (NH4)2SO4, 1 M Li2SO4, 0.1 M sodium citrate pH 5.5, 1 mM DTT, 1 mM EDTA, 1 mM NaN3
Resolution 2.60 Å R-free 0.320
7LCA Zoogloea ramigera biosynthetic thiolase Y218E/delH221 mutant Deposited 2021-01-10 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–392（391 aa）
Chain B 2–392（391 aa）
Chain C 2–392（391 aa）
Chain D 2–392（391 aa）
Mutation：Y218E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y218E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y218E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y218E Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 7 COA COENZYME A × 4 CL CHLORIDE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；289 K；1.3 M (NH4)2SO4, 0.5 M Li2SO4, 0.1 M sodium citrate pH 5.5, 1 mM DTT, 1 mM EDTA, 1 mM NaN3
Resolution 2.00 Å R-free 0.283
7LCL Zoogloea ramigera biosynthetic thiolase Q183Y mutant Deposited 2021-01-11 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–392（391 aa）
Chain B 2–392（391 aa）
Chain C 2–392（391 aa）
Chain D 2–392（391 aa）
Mutation：Q183Y Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Q183Y Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Q183Y Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Q183Y Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 11 COA COENZYME A × 4 NH4 AMMONIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；289 K；0.2 M (NH4)2SO4, 1 M Li2SO4, 0.1 M sodium citrate pH 5.5, 1 mM DTT, 1 mM EDTA, 1 mM NaN3
Resolution 2.29 Å R-free 0.265
7LD2 Zoogloea ramigera biosynthetic thiolase Q183Y mutant, RbCl soak Deposited 2021-01-12 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–392（391 aa）
Chain B 2–392（391 aa）
Chain C 2–392（391 aa）
Chain D 2–392（391 aa）
Mutation：Q183Y Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Q183Y Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Q183Y Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Q183Y Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 4 COA COENZYME A × 4 RB RUBIDIUM ION × 4 CL CHLORIDE ION × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；289 K；0.4 M (NH4)2SO4, 0.5 M Li2SO4, 0.1 M sodium citrate pH 5.5, 1 mM DTT, 1 mM EDTA, 1 mM NaN3
Resolution 2.80 Å R-free 0.271
7LDC Zoogloea ramigera biosynthetic thiolase Q183Y/Y218E mutant Deposited 2021-01-13 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–392（391 aa）
Chain B 2–392（391 aa）
Chain C 2–392（391 aa）
Chain D 2–392（391 aa）
Mutation：Q183Y/Y218E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Q183Y/Y218E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Q183Y/Y218E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Q183Y/Y218E Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 10 COA COENZYME A × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；289 K；0.44 M (NH4)2SO4, 1.76 M Li2SO4, 0.1 M sodium citrate pH 5.5, 1 mM DTT, 1 mM EDTA, 1 mM NaN3
Resolution 2.50 Å R-free 0.260
7LDT Zoogloea ramigera biosynthetic thiolase Q183Y/Y218E mutant, RbCl soak Deposited 2021-01-14 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–392（391 aa）
Chain B 2–392（391 aa）
Chain C 2–392（391 aa）
Chain D 2–392（391 aa）
Mutation：Q183Y/Y218E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Q183Y/Y218E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Q183Y/Y218E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Q183Y/Y218E Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 4 COA COENZYME A × 4 RB RUBIDIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；289 K；0.44 M (NH4)2SO4, 1.76 M Li2SO4, 0.1 M sodium citrate pH 5.5, 1 mM DTT, 1 mM EDTA, 1 mM NaN3
Resolution 2.60 Å R-free 0.238
7LDU Zoogloea ramigera biosynthetic thiolase Q183Y/Y218E/delH221 mutant Deposited 2021-01-14 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–392（391 aa）
Chain B 2–392（391 aa）
Chain C 2–392（391 aa）
Chain D 2–392（391 aa）
Mutation：Q183Y, Y218E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Q183Y, Y218E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Q183Y, Y218E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Q183Y, Y218E Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 8 COA COENZYME A × 4 CL CHLORIDE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；289 K；1.8 M Li2SO4, 0.1 M sodium citrate pH 5.5, 1 mM DTT, 1 mM EDTA, 1 mM NaN3
Resolution 2.85 Å R-free 0.282
7LDV Zoogloea ramigera biosynthetic thiolase Q183Y/Y218E/delH221/S227K mutant Deposited 2021-01-14 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–392（391 aa）
Chain B 2–392（391 aa）
Chain C 2–392（391 aa）
Chain D 2–392（391 aa）
Mutation：Q183Y, Y218E, S227K Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Q183Y, Y218E, S227K Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Q183Y, Y218E, S227K Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Q183Y, Y218E, S227K Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 10 COA COENZYME A × 4 NH4 AMMONIUM ION × 4 CL CHLORIDE ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；289 K；1.17 M (NH4)2SO4, 0.78 M Li2SO4, 0.1 M sodium citrate pH 5.5, 1 mM DTT, 1 mM EDTA, 1 mM NaN3
Resolution 2.90 Å R-free 0.234
7LDW Zoogloea ramigera biosynthetic thiolase Q183Y/Y218E/delH221/S227K/G248T mutant Deposited 2021-01-14 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–392（391 aa）
Chain B 2–392（391 aa）
Chain C 2–392（391 aa）
Chain D 2–392（391 aa）
Mutation：Q183Y, Y218E, S227K, G248T Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Q183Y, Y218E, S227K, G248T Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Q183Y, Y218E, S227K, G248T Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Q183Y, Y218E, S227K, G248T Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 10 COA COENZYME A × 4 NH4 AMMONIUM ION × 3 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；289 K；1.32 M (NH4)2SO4, 0.88 M Li2SO4, 0.1 M sodium citrate pH 5.5, 1 mM DTT, 1 mM EDTA, 1 mM NaN3
Resolution 2.50 Å R-free 0.247

30 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name THIL_ZOORA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–389； UniProt 5–392 Author chain B； PDBConstruct 1–389； UniProt 5–392 Author chain C； PDBConstruct 1–389； UniProt 5–392 Author chain D； PDBConstruct 1–389； UniProt 5–392

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 1dm3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1dm3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1dm3
Deposition date deposition_date1999-12-13
Structure title titleACETYLATED BIOSYNTHETIC THIOLASE FROM ZOOGLOEA RAMIGERA IN COMPLEX WITH ACETYL-COA
Keywords keywordsBIOSYNTHETIC THIOLASE, REACTION INTERMEDIATE, ACETYL-COA, BETA-ALPHA FOLD, ACETYL-COA ACETYLTRANSFERASE, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier37.52 Å
Radius of gyration Rg (electron density) rg_electron37.14 Å
Forward intensity I(0) i0449525000.00
Molecular weight molecular_weight164830.0 kDa
Excluded volume excluded_volume203180 ų
Envelope volume envelope_volume249350 ų
Hydration-shell volume shell_volume54609 ų
Envelope diameter envelope_diameter119.1 Å
Shell Rg shell_rg44.49 Å
Envelope Rg envelope_rg36.65 Å
Shape Rg shape_rg37.15 Å
Total Rg total_rg37.49 Å
Total atoms total_atoms11498
Residues n_residues1552
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax121.0 Å
Rg (real space) rg_real37.45 Å
Rg uncertainty (real space) rg_real_error0.94 Å
I(0) (real space) i0_real4.4950e+08
I(0) uncertainty (real space) i0_real_error8.2790e+06
Rg (reciprocal space) rg_reciprocal37.50 Å
I(0) (reciprocal space) i0_reciprocal449500000.0000
Solution quality estimate total_estimate0.9015
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.4 Å
Skewness Skewness skewness0.208
Kurtosis Kurtosis kurtosis-0.662
Angular range angular_range— – 0.2100 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha151000000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.924; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.945
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd1dm3a1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.95 — Thiolase-like
Superfamily Superfamily superfamilyc.95.1 — Thiolase-like
Family Family familyc.95.1.1 — Thiolase-related
Domain ID domain_idd1dm3a2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.95 — Thiolase-like
Superfamily Superfamily superfamilyc.95.1 — Thiolase-like
Family Family familyc.95.1.1 — Thiolase-related
Domain ID domain_idd1dm3b1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.95 — Thiolase-like
Superfamily Superfamily superfamilyc.95.1 — Thiolase-like
Family Family familyc.95.1.1 — Thiolase-related
Domain ID domain_idd1dm3b2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.95 — Thiolase-like
Superfamily Superfamily superfamilyc.95.1 — Thiolase-like
Family Family familyc.95.1.1 — Thiolase-related
Domain ID domain_idd1dm3c1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.95 — Thiolase-like
Superfamily Superfamily superfamilyc.95.1 — Thiolase-like
Family Family familyc.95.1.1 — Thiolase-related
Domain ID domain_idd1dm3c2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.95 — Thiolase-like
Superfamily Superfamily superfamilyc.95.1 — Thiolase-like
Family Family familyc.95.1.1 — Thiolase-related
Domain ID domain_idd1dm3d1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.95 — Thiolase-like
Superfamily Superfamily superfamilyc.95.1 — Thiolase-like
Family Family familyc.95.1.1 — Thiolase-related
Domain ID domain_idd1dm3d2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.95 — Thiolase-like
Superfamily Superfamily superfamilyc.95.1 — Thiolase-like
Family Family familyc.95.1.1 — Thiolase-related

CATH v4.4 (8 domains)

Domain ID domain_id1dm3A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology47 — Peroxisomal Thiolase; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Thiolase/Chalcone synthase
Domain ID domain_id1dm3A02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology47 — Peroxisomal Thiolase; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Thiolase/Chalcone synthase
Domain ID domain_id1dm3B01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology47 — Peroxisomal Thiolase; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Thiolase/Chalcone synthase
Domain ID domain_id1dm3B02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology47 — Peroxisomal Thiolase; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Thiolase/Chalcone synthase
Domain ID domain_id1dm3C01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology47 — Peroxisomal Thiolase; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Thiolase/Chalcone synthase
Domain ID domain_id1dm3C02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology47 — Peroxisomal Thiolase; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Thiolase/Chalcone synthase
Domain ID domain_id1dm3D01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology47 — Peroxisomal Thiolase; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Thiolase/Chalcone synthase
Domain ID domain_id1dm3D02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology47 — Peroxisomal Thiolase; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Thiolase/Chalcone synthase
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8. Citations (3)

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9. Files and Curves (10)