1c3o

CRYSTAL STRUCTURE OF THE CARBAMOYL PHOSPHATE SYNTHETASE: SMALL SUBUNIT MUTANT C269S WITH BOUND GLUTAMINE

Method: X-RAY DIFFRACTION D_max: 251.2 Å Quality: GOOD

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

CARBAMOYL PHOSPHATE SYNTHETASE: LARGE SUBUNIT

Escherichia coli

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 × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain A； UniProt 1–1073 Chain C； UniProt 1–1073 Chain E； UniProt 1–1073 Chain G； UniProt 1–1073	Not recorded	CARBAMOYL PHOSPHATE SYNTHETASE: SMALL SUBUNIT × 4 （P00907） MN MANGANESE (II) ION × 12 K POTASSIUM ION × 32 CL CHLORIDE ION × 16 PO4 PHOSPHATE ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 8 ORN L-ornithine × 4 GLN GLUTAMINE × 8 NET TETRAETHYLAMMONIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions：BATCH；pH 7.4；278 K；PEG-8000, MANGANESE CHLORIDE, TETRAETHYLAMMONIUM CHLORIDE, POTASSIUM CHLORIDE, BERYLLIUM FLUORIDE, ADENOSINE 5'-DIPHOSPHATE,L-ORNITHINE, L-GLUTAMINE, HEPPS, pH 7.4, BATCH, temperature 278K	Resolution 2.10 Å R-free 0.258

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 1C3O	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1A9X CARBAMOYL PHOSPHATE SYNTHETASE: CAUGHT IN THE ACT OF GLUTAMINE HYDROLYSIS Deposited 1998-04-14	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–1072（1072 aa） Chain C 1–1072（1072 aa） Chain E 1–1072（1072 aa） Chain G 1–1072（1072 aa）	Not recorded	PO4 PHOSPHATE ION × 15 MN MANGANESE (II) ION × 12 K POTASSIUM ION × 32 CL CHLORIDE ION × 28 ADP ADENOSINE-5'-DIPHOSPHATE × 8 ORN L-ornithine × 4 NET TETRAETHYLAMMONIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；0.65M NET4CL 8% PEG 8000 100MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 5MM GLUTAMINE 25MM HEPES PH 7.4 THEN SOAKED INTO: 1.4M NET4CL 8% PEG 8000 250MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 5MM GLUTAMINE 25MM HEPES PH 7.4 7.5% ETHYLENE GLYCOL	Resolution 1.80 Å
1A9X CARBAMOYL PHOSPHATE SYNTHETASE: CAUGHT IN THE ACT OF GLUTAMINE HYDROLYSIS Deposited 1998-04-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–1072（1072 aa）	Not recorded	PO4 PHOSPHATE ION × 4 MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；0.65M NET4CL 8% PEG 8000 100MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 5MM GLUTAMINE 25MM HEPES PH 7.4 THEN SOAKED INTO: 1.4M NET4CL 8% PEG 8000 250MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 5MM GLUTAMINE 25MM HEPES PH 7.4 7.5% ETHYLENE GLYCOL	Resolution 1.80 Å
1A9X CARBAMOYL PHOSPHATE SYNTHETASE: CAUGHT IN THE ACT OF GLUTAMINE HYDROLYSIS Deposited 1998-04-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain G 1–1072（1072 aa）	Not recorded	PO4 PHOSPHATE ION × 4 MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；0.65M NET4CL 8% PEG 8000 100MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 5MM GLUTAMINE 25MM HEPES PH 7.4 THEN SOAKED INTO: 1.4M NET4CL 8% PEG 8000 250MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 5MM GLUTAMINE 25MM HEPES PH 7.4 7.5% ETHYLENE GLYCOL	Resolution 1.80 Å
1A9X CARBAMOYL PHOSPHATE SYNTHETASE: CAUGHT IN THE ACT OF GLUTAMINE HYDROLYSIS Deposited 1998-04-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–1072（1072 aa）	Not recorded	PO4 PHOSPHATE ION × 4 MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；0.65M NET4CL 8% PEG 8000 100MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 5MM GLUTAMINE 25MM HEPES PH 7.4 THEN SOAKED INTO: 1.4M NET4CL 8% PEG 8000 250MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 5MM GLUTAMINE 25MM HEPES PH 7.4 7.5% ETHYLENE GLYCOL	Resolution 1.80 Å
1A9X CARBAMOYL PHOSPHATE SYNTHETASE: CAUGHT IN THE ACT OF GLUTAMINE HYDROLYSIS Deposited 1998-04-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 1–1072（1072 aa）	Not recorded	PO4 PHOSPHATE ION × 3 MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；0.65M NET4CL 8% PEG 8000 100MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 5MM GLUTAMINE 25MM HEPES PH 7.4 THEN SOAKED INTO: 1.4M NET4CL 8% PEG 8000 250MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 5MM GLUTAMINE 25MM HEPES PH 7.4 7.5% ETHYLENE GLYCOL	Resolution 1.80 Å
1BXR STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE COMPLEXED WITH THE ATP ANALOG AMPPNP Deposited 1998-10-08	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–1072（1072 aa） Chain C 1–1072（1072 aa） Chain E 1–1072（1072 aa） Chain G 1–1072（1072 aa）	Not recorded	MN MANGANESE (II) ION × 13 K POTASSIUM ION × 19 CL CHLORIDE ION × 14 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 8 ORN L-ornithine × 4 NET TETRAETHYLAMMONIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；pH 7.4	Resolution 2.10 Å
1BXR STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE COMPLEXED WITH THE ATP ANALOG AMPPNP Deposited 1998-10-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 1–1072（1072 aa）	Not recorded	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 5 CL CHLORIDE ION × 2 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；pH 7.4	Resolution 2.10 Å
1BXR STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE COMPLEXED WITH THE ATP ANALOG AMPPNP Deposited 1998-10-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–1072（1072 aa）	Not recorded	MN MANGANESE (II) ION × 4 K POTASSIUM ION × 5 CL CHLORIDE ION × 4 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；pH 7.4	Resolution 2.10 Å
1BXR STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE COMPLEXED WITH THE ATP ANALOG AMPPNP Deposited 1998-10-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–1072（1072 aa）	Not recorded	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 4 CL CHLORIDE ION × 4 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；pH 7.4	Resolution 2.10 Å
1BXR STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE COMPLEXED WITH THE ATP ANALOG AMPPNP Deposited 1998-10-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain G 1–1072（1072 aa）	Not recorded	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 5 CL CHLORIDE ION × 4 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；pH 7.4	Resolution 2.10 Å
1C30 CRYSTAL STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE: SMALL SUBUNIT MUTATION C269S Deposited 1999-07-24	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–1073（1073 aa） Chain C 1–1073（1073 aa） Chain E 1–1073（1073 aa） Chain G 1–1073（1073 aa）	Not recorded	MN MANGANESE (II) ION × 12 K POTASSIUM ION × 32 CL CHLORIDE ION × 16 PO4 PHOSPHATE ION × 6 ORN L-ornithine × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 8 NET TETRAETHYLAMMONIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions BATCH；pH 7.4；277 K；PEG 8000, POTASSIUM CHLORIDE, MANGANESE CHLORIDE, TETRAETHYLAMMONIUM CHLORIDE, L-ORNITHINE, ADP, BERYLLIUM FLUORIDE, HEPPS, pH 7.4, BATCH, temperature 277.0K	Resolution 2.00 Å R-free 0.246
1C30 CRYSTAL STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE: SMALL SUBUNIT MUTATION C269S Deposited 1999-07-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain G 1–1073（1073 aa）	Not recorded	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 4 PO4 PHOSPHATE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions BATCH；pH 7.4；277 K；PEG 8000, POTASSIUM CHLORIDE, MANGANESE CHLORIDE, TETRAETHYLAMMONIUM CHLORIDE, L-ORNITHINE, ADP, BERYLLIUM FLUORIDE, HEPPS, pH 7.4, BATCH, temperature 277.0K	Resolution 2.00 Å R-free 0.246
1C30 CRYSTAL STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE: SMALL SUBUNIT MUTATION C269S Deposited 1999-07-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–1073（1073 aa）	Not recorded	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 4 PO4 PHOSPHATE ION × 1 ORN L-ornithine × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions BATCH；pH 7.4；277 K；PEG 8000, POTASSIUM CHLORIDE, MANGANESE CHLORIDE, TETRAETHYLAMMONIUM CHLORIDE, L-ORNITHINE, ADP, BERYLLIUM FLUORIDE, HEPPS, pH 7.4, BATCH, temperature 277.0K	Resolution 2.00 Å R-free 0.246
1C30 CRYSTAL STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE: SMALL SUBUNIT MUTATION C269S Deposited 1999-07-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–1073（1073 aa）	Not recorded	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 4 PO4 PHOSPHATE ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions BATCH；pH 7.4；277 K；PEG 8000, POTASSIUM CHLORIDE, MANGANESE CHLORIDE, TETRAETHYLAMMONIUM CHLORIDE, L-ORNITHINE, ADP, BERYLLIUM FLUORIDE, HEPPS, pH 7.4, BATCH, temperature 277.0K	Resolution 2.00 Å R-free 0.246
1C30 CRYSTAL STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE: SMALL SUBUNIT MUTATION C269S Deposited 1999-07-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 1–1073（1073 aa）	Not recorded	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 4 PO4 PHOSPHATE ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions BATCH；pH 7.4；277 K；PEG 8000, POTASSIUM CHLORIDE, MANGANESE CHLORIDE, TETRAETHYLAMMONIUM CHLORIDE, L-ORNITHINE, ADP, BERYLLIUM FLUORIDE, HEPPS, pH 7.4, BATCH, temperature 277.0K	Resolution 2.00 Å R-free 0.246
1CE8 CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIS COLI WITH COMPLEXED WITH THE ALLOSTERIC LIGAND IMP Deposited 1999-03-18	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–1073（1073 aa） Chain C 1–1073（1073 aa） Chain E 1–1073（1073 aa） Chain G 1–1073（1073 aa）	Not recorded	MN MANGANESE (II) ION × 12 K POTASSIUM ION × 28 CL CHLORIDE ION × 12 PO4 PHOSPHATE ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 8 ORN L-ornithine × 8 IMP INOSINIC ACID × 4 NET TETRAETHYLAMMONIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；pH 7.4	Resolution 2.10 Å R-free 0.250
1CE8 CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIS COLI WITH COMPLEXED WITH THE ALLOSTERIC LIGAND IMP Deposited 1999-03-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–1073（1073 aa）	Not recorded	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 7 CL CHLORIDE ION × 3 PO4 PHOSPHATE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 2 IMP INOSINIC ACID × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；pH 7.4	Resolution 2.10 Å R-free 0.250
1CE8 CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIS COLI WITH COMPLEXED WITH THE ALLOSTERIC LIGAND IMP Deposited 1999-03-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain G 1–1073（1073 aa）	Not recorded	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 7 CL CHLORIDE ION × 3 PO4 PHOSPHATE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 2 IMP INOSINIC ACID × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；pH 7.4	Resolution 2.10 Å R-free 0.250
1CE8 CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIS COLI WITH COMPLEXED WITH THE ALLOSTERIC LIGAND IMP Deposited 1999-03-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–1073（1073 aa）	Not recorded	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 7 CL CHLORIDE ION × 3 PO4 PHOSPHATE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 2 IMP INOSINIC ACID × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；pH 7.4	Resolution 2.10 Å R-free 0.250
1CE8 CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIS COLI WITH COMPLEXED WITH THE ALLOSTERIC LIGAND IMP Deposited 1999-03-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 1–1073（1073 aa）	Not recorded	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 7 CL CHLORIDE ION × 3 PO4 PHOSPHATE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 2 IMP INOSINIC ACID × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；pH 7.4	Resolution 2.10 Å R-free 0.250
1CS0 Crystal structure of carbamoyl phosphate synthetase complexed at CYS269 in the small subunit with the tetrahedral mimic l-glutamate gamma-semialdehyde Deposited 1999-08-16	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–1073（1073 aa） Chain C 1–1073（1073 aa） Chain E 1–1073（1073 aa） Chain G 1–1073（1073 aa）	Not recorded	MN MANGANESE (II) ION × 12 K POTASSIUM ION × 33 CL CHLORIDE ION × 29 PO4 PHOSPHATE ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 8 ORN L-ornithine × 4 NET TETRAETHYLAMMONIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions BATCH；pH 7.4；277 K；PEG 8000, TETRAETHYLAMMONIUM CHLORIDE, POTASSIUM CHLORIDE, MANGANESE(II) CHLORIDE, ADENOSINE 5'-DIPHOSPHATE, L-ORNITHINE, L-GLUTAMATE GAMMA-SEMIALDEHYDE, pH 7.4, BATCH, temperature 277K	Resolution 2.00 Å R-free 0.242
1CS0 Crystal structure of carbamoyl phosphate synthetase complexed at CYS269 in the small subunit with the tetrahedral mimic l-glutamate gamma-semialdehyde Deposited 1999-08-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–1073（1073 aa）	Not recorded	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 7 PO4 PHOSPHATE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions BATCH；pH 7.4；277 K；PEG 8000, TETRAETHYLAMMONIUM CHLORIDE, POTASSIUM CHLORIDE, MANGANESE(II) CHLORIDE, ADENOSINE 5'-DIPHOSPHATE, L-ORNITHINE, L-GLUTAMATE GAMMA-SEMIALDEHYDE, pH 7.4, BATCH, temperature 277K	Resolution 2.00 Å R-free 0.242
1CS0 Crystal structure of carbamoyl phosphate synthetase complexed at CYS269 in the small subunit with the tetrahedral mimic l-glutamate gamma-semialdehyde Deposited 1999-08-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain G 1–1073（1073 aa）	Not recorded	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 7 PO4 PHOSPHATE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions BATCH；pH 7.4；277 K；PEG 8000, TETRAETHYLAMMONIUM CHLORIDE, POTASSIUM CHLORIDE, MANGANESE(II) CHLORIDE, ADENOSINE 5'-DIPHOSPHATE, L-ORNITHINE, L-GLUTAMATE GAMMA-SEMIALDEHYDE, pH 7.4, BATCH, temperature 277K	Resolution 2.00 Å R-free 0.242
1CS0 Crystal structure of carbamoyl phosphate synthetase complexed at CYS269 in the small subunit with the tetrahedral mimic l-glutamate gamma-semialdehyde Deposited 1999-08-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–1073（1073 aa）	Not recorded	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 8 PO4 PHOSPHATE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions BATCH；pH 7.4；277 K；PEG 8000, TETRAETHYLAMMONIUM CHLORIDE, POTASSIUM CHLORIDE, MANGANESE(II) CHLORIDE, ADENOSINE 5'-DIPHOSPHATE, L-ORNITHINE, L-GLUTAMATE GAMMA-SEMIALDEHYDE, pH 7.4, BATCH, temperature 277K	Resolution 2.00 Å R-free 0.242
1CS0 Crystal structure of carbamoyl phosphate synthetase complexed at CYS269 in the small subunit with the tetrahedral mimic l-glutamate gamma-semialdehyde Deposited 1999-08-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 1–1073（1073 aa）	Not recorded	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 9 CL CHLORIDE ION × 7 PO4 PHOSPHATE ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions BATCH；pH 7.4；277 K；PEG 8000, TETRAETHYLAMMONIUM CHLORIDE, POTASSIUM CHLORIDE, MANGANESE(II) CHLORIDE, ADENOSINE 5'-DIPHOSPHATE, L-ORNITHINE, L-GLUTAMATE GAMMA-SEMIALDEHYDE, pH 7.4, BATCH, temperature 277K	Resolution 2.00 Å R-free 0.242
1JDB CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIA COLI Deposited 1997-03-25	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain B 1–1072（1072 aa） Chain E 1–1072（1072 aa） Chain H 1–1072（1072 aa） Chain K 1–1072（1072 aa）	Not recorded	MN MANGANESE (II) ION × 16 K POTASSIUM ION × 29 PO4 PHOSPHATE ION × 9 CL CHLORIDE ION × 29 GLN GLUTAMINE × 8 ADP ADENOSINE-5'-DIPHOSPHATE × 8 ORN L-ornithine × 4 NET TETRAETHYLAMMONIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；0.65M TETRAETHYL AMMONIUM CHLORIDE (E4NCL) 8% PEG 8000 100MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 25MM HEPES PH 7.4. THE CRYSTAL WAS SOAKED INTO: 1.4M E4NCL 8% PEG 8000 250MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 25MM GLUTAMINE 25MM HEPES PH 7.4 7.5% ETHYLENE GLYCOL.	Resolution 2.10 Å
1JDB CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIA COLI Deposited 1997-03-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–1072（1072 aa）	Not recorded	MN MANGANESE (II) ION × 4 K POTASSIUM ION × 7 PO4 PHOSPHATE ION × 2 CL CHLORIDE ION × 7 GLN GLUTAMINE × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；0.65M TETRAETHYL AMMONIUM CHLORIDE (E4NCL) 8% PEG 8000 100MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 25MM HEPES PH 7.4. THE CRYSTAL WAS SOAKED INTO: 1.4M E4NCL 8% PEG 8000 250MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 25MM GLUTAMINE 25MM HEPES PH 7.4 7.5% ETHYLENE GLYCOL.	Resolution 2.10 Å
1JDB CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIA COLI Deposited 1997-03-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 1–1072（1072 aa）	Not recorded	MN MANGANESE (II) ION × 4 K POTASSIUM ION × 6 PO4 PHOSPHATE ION × 2 CL CHLORIDE ION × 7 GLN GLUTAMINE × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；0.65M TETRAETHYL AMMONIUM CHLORIDE (E4NCL) 8% PEG 8000 100MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 25MM HEPES PH 7.4. THE CRYSTAL WAS SOAKED INTO: 1.4M E4NCL 8% PEG 8000 250MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 25MM GLUTAMINE 25MM HEPES PH 7.4 7.5% ETHYLENE GLYCOL.	Resolution 2.10 Å
1JDB CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIA COLI Deposited 1997-03-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain K 1–1072（1072 aa）	Not recorded	MN MANGANESE (II) ION × 4 K POTASSIUM ION × 8 PO4 PHOSPHATE ION × 3 CL CHLORIDE ION × 7 GLN GLUTAMINE × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；0.65M TETRAETHYL AMMONIUM CHLORIDE (E4NCL) 8% PEG 8000 100MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 25MM HEPES PH 7.4. THE CRYSTAL WAS SOAKED INTO: 1.4M E4NCL 8% PEG 8000 250MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 25MM GLUTAMINE 25MM HEPES PH 7.4 7.5% ETHYLENE GLYCOL.	Resolution 2.10 Å
1JDB CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIA COLI Deposited 1997-03-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 1–1072（1072 aa）	Not recorded	MN MANGANESE (II) ION × 4 K POTASSIUM ION × 8 PO4 PHOSPHATE ION × 2 CL CHLORIDE ION × 8 GLN GLUTAMINE × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；0.65M TETRAETHYL AMMONIUM CHLORIDE (E4NCL) 8% PEG 8000 100MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 25MM HEPES PH 7.4. THE CRYSTAL WAS SOAKED INTO: 1.4M E4NCL 8% PEG 8000 250MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 25MM GLUTAMINE 25MM HEPES PH 7.4 7.5% ETHYLENE GLYCOL.	Resolution 2.10 Å
1KEE Inactivation of the Amidotransferase Activity of Carbamoyl Phosphate Synthetase by the Antibiotic Acivicin Deposited 2001-11-15	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 0–1072（1073 aa） Chain C 0–1072（1073 aa） Chain E 0–1072（1073 aa） Chain G 0–1072（1073 aa）	Not recorded	MN MANGANESE (II) ION × 12 K POTASSIUM ION × 32 CL CHLORIDE ION × 22 PO4 PHOSPHATE ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 8 ORN L-ornithine × 4 NET TETRAETHYLAMMONIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions batch；pH 7.4；277 K；PEG 8000, Hepes, potassium chloride, manganese chloride, ornithine, tetraethylammonium chloride, HEPPS, pH 7.4, batch, temperature 277K	Resolution 2.10 Å R-free 0.211
1KEE Inactivation of the Amidotransferase Activity of Carbamoyl Phosphate Synthetase by the Antibiotic Acivicin Deposited 2001-11-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain G 0–1072（1073 aa）	Not recorded	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 5 PO4 PHOSPHATE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions batch；pH 7.4；277 K；PEG 8000, Hepes, potassium chloride, manganese chloride, ornithine, tetraethylammonium chloride, HEPPS, pH 7.4, batch, temperature 277K	Resolution 2.10 Å R-free 0.211
1KEE Inactivation of the Amidotransferase Activity of Carbamoyl Phosphate Synthetase by the Antibiotic Acivicin Deposited 2001-11-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 0–1072（1073 aa）	Not recorded	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 5 PO4 PHOSPHATE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions batch；pH 7.4；277 K；PEG 8000, Hepes, potassium chloride, manganese chloride, ornithine, tetraethylammonium chloride, HEPPS, pH 7.4, batch, temperature 277K	Resolution 2.10 Å R-free 0.211
1KEE Inactivation of the Amidotransferase Activity of Carbamoyl Phosphate Synthetase by the Antibiotic Acivicin Deposited 2001-11-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 0–1072（1073 aa）	Not recorded	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 6 PO4 PHOSPHATE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions batch；pH 7.4；277 K；PEG 8000, Hepes, potassium chloride, manganese chloride, ornithine, tetraethylammonium chloride, HEPPS, pH 7.4, batch, temperature 277K	Resolution 2.10 Å R-free 0.211
1KEE Inactivation of the Amidotransferase Activity of Carbamoyl Phosphate Synthetase by the Antibiotic Acivicin Deposited 2001-11-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 0–1072（1073 aa）	Not recorded	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 6 PO4 PHOSPHATE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions batch；pH 7.4；277 K；PEG 8000, Hepes, potassium chloride, manganese chloride, ornithine, tetraethylammonium chloride, HEPPS, pH 7.4, batch, temperature 277K	Resolution 2.10 Å R-free 0.211
1M6V Crystal Structure of the G359F (small subunit) Point Mutant of Carbamoyl Phosphate Synthetase Deposited 2002-07-17	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 0–1072（1073 aa） Chain C 0–1072（1073 aa） Chain E 0–1072（1073 aa） Chain G 0–1072（1073 aa）	Not recorded	MN MANGANESE (II) ION × 12 K POTASSIUM ION × 26 CL CHLORIDE ION × 28 PO4 PHOSPHATE ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 8 ORN L-ornithine × 4 NET TETRAETHYLAMMONIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions batch；pH 7.4；277 K；PEG-8000, manganese chloride, potassium chloride, ADP, ornithine, tetraethylammonium chloride, HEPPS, pH 7.4, batch, temperature 277K	Resolution 2.10 Å R-free 0.245
1T36 Crystal structure of E. coli carbamoyl phosphate synthetase small subunit mutant C248D complexed with uridine 5'-monophosphate Deposited 2004-04-24	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 0–1072（1073 aa） Chain C 0–1072（1073 aa） Chain E 0–1072（1073 aa） Chain G 0–1072（1073 aa）	Not recorded	MN MANGANESE (II) ION × 12 K POTASSIUM ION × 22 PO4 PHOSPHATE ION × 5 CL CHLORIDE ION × 27 ADP ADENOSINE-5'-DIPHOSPHATE × 8 ORN L-ornithine × 4 NET TETRAETHYLAMMONIUM ION × 4 U5P URIDINE-5'-MONOPHOSPHATE × 4	X-RAY DIFFRACTION X-ray crystallization conditions batch；pH 7.4；277 K；PEG 8000, tetramethylammonium chloride, potassium chloride, manganese chloride, ornithine, ADP, HEPES, pH 7.4, batch, temperature 277K	Resolution 2.10 Å R-free 0.209

9 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CARB_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–1073； UniProt 1–1073 Author chain C； PDBConstruct 1–1073； UniProt 1–1073 Author chain E； PDBConstruct 1–1073； UniProt 1–1073 Author chain G； PDBConstruct 1–1073； UniProt 1–1073

CARBAMOYL PHOSPHATE SYNTHETASE: SMALL SUBUNIT

Escherichia coli

UniProt P00907

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 × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain B； UniProt 1–382 Chain D； UniProt 1–382 Chain F； UniProt 1–382 Chain H； UniProt 1–382	Mutation：C269S	CARBAMOYL PHOSPHATE SYNTHETASE: LARGE SUBUNIT × 4 （P00968） MN MANGANESE (II) ION × 12 K POTASSIUM ION × 32 CL CHLORIDE ION × 16 PO4 PHOSPHATE ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 8 ORN L-ornithine × 4 GLN GLUTAMINE × 8 NET TETRAETHYLAMMONIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions：BATCH；pH 7.4；278 K；PEG-8000, MANGANESE CHLORIDE, TETRAETHYLAMMONIUM CHLORIDE, POTASSIUM CHLORIDE, BERYLLIUM FLUORIDE, ADENOSINE 5'-DIPHOSPHATE,L-ORNITHINE, L-GLUTAMINE, HEPPS, pH 7.4, BATCH, temperature 278K	Resolution 2.10 Å R-free 0.258

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 1C3O	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1A9X CARBAMOYL PHOSPHATE SYNTHETASE: CAUGHT IN THE ACT OF GLUTAMINE HYDROLYSIS Deposited 1998-04-14	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain B 2–380（379 aa） Chain D 2–380（379 aa） Chain F 2–380（379 aa） Chain H 2–380（379 aa）	Mutation：H353N Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：H353N Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：H353N Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：H353N Non-standard monomer：Yes (specific site not provided by mmCIF)	PO4 PHOSPHATE ION × 15 MN MANGANESE (II) ION × 12 K POTASSIUM ION × 32 CL CHLORIDE ION × 28 ADP ADENOSINE-5'-DIPHOSPHATE × 8 ORN L-ornithine × 4 NET TETRAETHYLAMMONIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；0.65M NET4CL 8% PEG 8000 100MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 5MM GLUTAMINE 25MM HEPES PH 7.4 THEN SOAKED INTO: 1.4M NET4CL 8% PEG 8000 250MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 5MM GLUTAMINE 25MM HEPES PH 7.4 7.5% ETHYLENE GLYCOL	Resolution 1.80 Å
1A9X CARBAMOYL PHOSPHATE SYNTHETASE: CAUGHT IN THE ACT OF GLUTAMINE HYDROLYSIS Deposited 1998-04-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 2–380（379 aa）	Mutation：H353N Non-standard monomer：Yes (specific site not provided by mmCIF)	PO4 PHOSPHATE ION × 4 MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；0.65M NET4CL 8% PEG 8000 100MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 5MM GLUTAMINE 25MM HEPES PH 7.4 THEN SOAKED INTO: 1.4M NET4CL 8% PEG 8000 250MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 5MM GLUTAMINE 25MM HEPES PH 7.4 7.5% ETHYLENE GLYCOL	Resolution 1.80 Å
1A9X CARBAMOYL PHOSPHATE SYNTHETASE: CAUGHT IN THE ACT OF GLUTAMINE HYDROLYSIS Deposited 1998-04-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 2–380（379 aa）	Mutation：H353N Non-standard monomer：Yes (specific site not provided by mmCIF)	PO4 PHOSPHATE ION × 4 MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；0.65M NET4CL 8% PEG 8000 100MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 5MM GLUTAMINE 25MM HEPES PH 7.4 THEN SOAKED INTO: 1.4M NET4CL 8% PEG 8000 250MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 5MM GLUTAMINE 25MM HEPES PH 7.4 7.5% ETHYLENE GLYCOL	Resolution 1.80 Å
1A9X CARBAMOYL PHOSPHATE SYNTHETASE: CAUGHT IN THE ACT OF GLUTAMINE HYDROLYSIS Deposited 1998-04-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 2–380（379 aa）	Mutation：H353N Non-standard monomer：Yes (specific site not provided by mmCIF)	PO4 PHOSPHATE ION × 4 MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；0.65M NET4CL 8% PEG 8000 100MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 5MM GLUTAMINE 25MM HEPES PH 7.4 THEN SOAKED INTO: 1.4M NET4CL 8% PEG 8000 250MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 5MM GLUTAMINE 25MM HEPES PH 7.4 7.5% ETHYLENE GLYCOL	Resolution 1.80 Å
1A9X CARBAMOYL PHOSPHATE SYNTHETASE: CAUGHT IN THE ACT OF GLUTAMINE HYDROLYSIS Deposited 1998-04-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 2–380（379 aa）	Mutation：H353N Non-standard monomer：Yes (specific site not provided by mmCIF)	PO4 PHOSPHATE ION × 3 MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；0.65M NET4CL 8% PEG 8000 100MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 5MM GLUTAMINE 25MM HEPES PH 7.4 THEN SOAKED INTO: 1.4M NET4CL 8% PEG 8000 250MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 5MM GLUTAMINE 25MM HEPES PH 7.4 7.5% ETHYLENE GLYCOL	Resolution 1.80 Å
1C30 CRYSTAL STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE: SMALL SUBUNIT MUTATION C269S Deposited 1999-07-24	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain B 1–382（382 aa） Chain D 1–382（382 aa） Chain F 1–382（382 aa） Chain H 1–382（382 aa）	Mutation：C269S Mutation：C269S Mutation：C269S Mutation：C269S	MN MANGANESE (II) ION × 12 K POTASSIUM ION × 32 CL CHLORIDE ION × 16 PO4 PHOSPHATE ION × 6 ORN L-ornithine × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 8 NET TETRAETHYLAMMONIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions BATCH；pH 7.4；277 K；PEG 8000, POTASSIUM CHLORIDE, MANGANESE CHLORIDE, TETRAETHYLAMMONIUM CHLORIDE, L-ORNITHINE, ADP, BERYLLIUM FLUORIDE, HEPPS, pH 7.4, BATCH, temperature 277.0K	Resolution 2.00 Å R-free 0.246
1C30 CRYSTAL STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE: SMALL SUBUNIT MUTATION C269S Deposited 1999-07-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 1–382（382 aa）	Mutation：C269S	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 4 PO4 PHOSPHATE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions BATCH；pH 7.4；277 K；PEG 8000, POTASSIUM CHLORIDE, MANGANESE CHLORIDE, TETRAETHYLAMMONIUM CHLORIDE, L-ORNITHINE, ADP, BERYLLIUM FLUORIDE, HEPPS, pH 7.4, BATCH, temperature 277.0K	Resolution 2.00 Å R-free 0.246
1C30 CRYSTAL STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE: SMALL SUBUNIT MUTATION C269S Deposited 1999-07-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–382（382 aa）	Mutation：C269S	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 4 PO4 PHOSPHATE ION × 1 ORN L-ornithine × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions BATCH；pH 7.4；277 K；PEG 8000, POTASSIUM CHLORIDE, MANGANESE CHLORIDE, TETRAETHYLAMMONIUM CHLORIDE, L-ORNITHINE, ADP, BERYLLIUM FLUORIDE, HEPPS, pH 7.4, BATCH, temperature 277.0K	Resolution 2.00 Å R-free 0.246
1C30 CRYSTAL STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE: SMALL SUBUNIT MUTATION C269S Deposited 1999-07-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–382（382 aa）	Mutation：C269S	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 4 PO4 PHOSPHATE ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions BATCH；pH 7.4；277 K；PEG 8000, POTASSIUM CHLORIDE, MANGANESE CHLORIDE, TETRAETHYLAMMONIUM CHLORIDE, L-ORNITHINE, ADP, BERYLLIUM FLUORIDE, HEPPS, pH 7.4, BATCH, temperature 277.0K	Resolution 2.00 Å R-free 0.246
1C30 CRYSTAL STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE: SMALL SUBUNIT MUTATION C269S Deposited 1999-07-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 1–382（382 aa）	Mutation：C269S	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 4 PO4 PHOSPHATE ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions BATCH；pH 7.4；277 K；PEG 8000, POTASSIUM CHLORIDE, MANGANESE CHLORIDE, TETRAETHYLAMMONIUM CHLORIDE, L-ORNITHINE, ADP, BERYLLIUM FLUORIDE, HEPPS, pH 7.4, BATCH, temperature 277.0K	Resolution 2.00 Å R-free 0.246
1CS0 Crystal structure of carbamoyl phosphate synthetase complexed at CYS269 in the small subunit with the tetrahedral mimic l-glutamate gamma-semialdehyde Deposited 1999-08-16	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain B 1–382（382 aa） Chain D 1–382（382 aa） Chain F 1–382（382 aa） Chain H 1–382（382 aa）	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)	MN MANGANESE (II) ION × 12 K POTASSIUM ION × 33 CL CHLORIDE ION × 29 PO4 PHOSPHATE ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 8 ORN L-ornithine × 4 NET TETRAETHYLAMMONIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions BATCH；pH 7.4；277 K；PEG 8000, TETRAETHYLAMMONIUM CHLORIDE, POTASSIUM CHLORIDE, MANGANESE(II) CHLORIDE, ADENOSINE 5'-DIPHOSPHATE, L-ORNITHINE, L-GLUTAMATE GAMMA-SEMIALDEHYDE, pH 7.4, BATCH, temperature 277K	Resolution 2.00 Å R-free 0.242
1CS0 Crystal structure of carbamoyl phosphate synthetase complexed at CYS269 in the small subunit with the tetrahedral mimic l-glutamate gamma-semialdehyde Deposited 1999-08-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–382（382 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 7 PO4 PHOSPHATE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions BATCH；pH 7.4；277 K；PEG 8000, TETRAETHYLAMMONIUM CHLORIDE, POTASSIUM CHLORIDE, MANGANESE(II) CHLORIDE, ADENOSINE 5'-DIPHOSPHATE, L-ORNITHINE, L-GLUTAMATE GAMMA-SEMIALDEHYDE, pH 7.4, BATCH, temperature 277K	Resolution 2.00 Å R-free 0.242
1CS0 Crystal structure of carbamoyl phosphate synthetase complexed at CYS269 in the small subunit with the tetrahedral mimic l-glutamate gamma-semialdehyde Deposited 1999-08-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 1–382（382 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 7 PO4 PHOSPHATE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions BATCH；pH 7.4；277 K；PEG 8000, TETRAETHYLAMMONIUM CHLORIDE, POTASSIUM CHLORIDE, MANGANESE(II) CHLORIDE, ADENOSINE 5'-DIPHOSPHATE, L-ORNITHINE, L-GLUTAMATE GAMMA-SEMIALDEHYDE, pH 7.4, BATCH, temperature 277K	Resolution 2.00 Å R-free 0.242
1CS0 Crystal structure of carbamoyl phosphate synthetase complexed at CYS269 in the small subunit with the tetrahedral mimic l-glutamate gamma-semialdehyde Deposited 1999-08-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–382（382 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 8 PO4 PHOSPHATE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions BATCH；pH 7.4；277 K；PEG 8000, TETRAETHYLAMMONIUM CHLORIDE, POTASSIUM CHLORIDE, MANGANESE(II) CHLORIDE, ADENOSINE 5'-DIPHOSPHATE, L-ORNITHINE, L-GLUTAMATE GAMMA-SEMIALDEHYDE, pH 7.4, BATCH, temperature 277K	Resolution 2.00 Å R-free 0.242
1CS0 Crystal structure of carbamoyl phosphate synthetase complexed at CYS269 in the small subunit with the tetrahedral mimic l-glutamate gamma-semialdehyde Deposited 1999-08-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 1–382（382 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 9 CL CHLORIDE ION × 7 PO4 PHOSPHATE ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions BATCH；pH 7.4；277 K；PEG 8000, TETRAETHYLAMMONIUM CHLORIDE, POTASSIUM CHLORIDE, MANGANESE(II) CHLORIDE, ADENOSINE 5'-DIPHOSPHATE, L-ORNITHINE, L-GLUTAMATE GAMMA-SEMIALDEHYDE, pH 7.4, BATCH, temperature 277K	Resolution 2.00 Å R-free 0.242
1JDB CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIA COLI Deposited 1997-03-25	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain C 1–382（382 aa） Chain F 1–382（382 aa） Chain I 1–382（382 aa） Chain L 1–382（382 aa）	Not recorded	MN MANGANESE (II) ION × 16 K POTASSIUM ION × 29 PO4 PHOSPHATE ION × 9 CL CHLORIDE ION × 29 GLN GLUTAMINE × 8 ADP ADENOSINE-5'-DIPHOSPHATE × 8 ORN L-ornithine × 4 NET TETRAETHYLAMMONIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；0.65M TETRAETHYL AMMONIUM CHLORIDE (E4NCL) 8% PEG 8000 100MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 25MM HEPES PH 7.4. THE CRYSTAL WAS SOAKED INTO: 1.4M E4NCL 8% PEG 8000 250MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 25MM GLUTAMINE 25MM HEPES PH 7.4 7.5% ETHYLENE GLYCOL.	Resolution 2.10 Å
1JDB CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIA COLI Deposited 1997-03-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–382（382 aa）	Not recorded	MN MANGANESE (II) ION × 4 K POTASSIUM ION × 7 PO4 PHOSPHATE ION × 2 CL CHLORIDE ION × 7 GLN GLUTAMINE × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；0.65M TETRAETHYL AMMONIUM CHLORIDE (E4NCL) 8% PEG 8000 100MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 25MM HEPES PH 7.4. THE CRYSTAL WAS SOAKED INTO: 1.4M E4NCL 8% PEG 8000 250MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 25MM GLUTAMINE 25MM HEPES PH 7.4 7.5% ETHYLENE GLYCOL.	Resolution 2.10 Å
1JDB CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIA COLI Deposited 1997-03-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain I 1–382（382 aa）	Not recorded	MN MANGANESE (II) ION × 4 K POTASSIUM ION × 6 PO4 PHOSPHATE ION × 2 CL CHLORIDE ION × 7 GLN GLUTAMINE × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；0.65M TETRAETHYL AMMONIUM CHLORIDE (E4NCL) 8% PEG 8000 100MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 25MM HEPES PH 7.4. THE CRYSTAL WAS SOAKED INTO: 1.4M E4NCL 8% PEG 8000 250MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 25MM GLUTAMINE 25MM HEPES PH 7.4 7.5% ETHYLENE GLYCOL.	Resolution 2.10 Å
1JDB CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIA COLI Deposited 1997-03-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain L 1–382（382 aa）	Not recorded	MN MANGANESE (II) ION × 4 K POTASSIUM ION × 8 PO4 PHOSPHATE ION × 3 CL CHLORIDE ION × 7 GLN GLUTAMINE × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；0.65M TETRAETHYL AMMONIUM CHLORIDE (E4NCL) 8% PEG 8000 100MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 25MM HEPES PH 7.4. THE CRYSTAL WAS SOAKED INTO: 1.4M E4NCL 8% PEG 8000 250MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 25MM GLUTAMINE 25MM HEPES PH 7.4 7.5% ETHYLENE GLYCOL.	Resolution 2.10 Å
1JDB CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIA COLI Deposited 1997-03-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 1–382（382 aa）	Not recorded	MN MANGANESE (II) ION × 4 K POTASSIUM ION × 8 PO4 PHOSPHATE ION × 2 CL CHLORIDE ION × 8 GLN GLUTAMINE × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；0.65M TETRAETHYL AMMONIUM CHLORIDE (E4NCL) 8% PEG 8000 100MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 25MM HEPES PH 7.4. THE CRYSTAL WAS SOAKED INTO: 1.4M E4NCL 8% PEG 8000 250MM KCL 2.5MM MNCL2 2.5MM ADP 2.5MM ORNITHINE 25MM GLUTAMINE 25MM HEPES PH 7.4 7.5% ETHYLENE GLYCOL.	Resolution 2.10 Å
1KEE Inactivation of the Amidotransferase Activity of Carbamoyl Phosphate Synthetase by the Antibiotic Acivicin Deposited 2001-11-15	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain B 1–382（382 aa） Chain D 1–382（382 aa） Chain F 1–382（382 aa） Chain H 1–382（382 aa）	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)	MN MANGANESE (II) ION × 12 K POTASSIUM ION × 32 CL CHLORIDE ION × 22 PO4 PHOSPHATE ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 8 ORN L-ornithine × 4 NET TETRAETHYLAMMONIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions batch；pH 7.4；277 K；PEG 8000, Hepes, potassium chloride, manganese chloride, ornithine, tetraethylammonium chloride, HEPPS, pH 7.4, batch, temperature 277K	Resolution 2.10 Å R-free 0.211
1KEE Inactivation of the Amidotransferase Activity of Carbamoyl Phosphate Synthetase by the Antibiotic Acivicin Deposited 2001-11-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 1–382（382 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 5 PO4 PHOSPHATE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions batch；pH 7.4；277 K；PEG 8000, Hepes, potassium chloride, manganese chloride, ornithine, tetraethylammonium chloride, HEPPS, pH 7.4, batch, temperature 277K	Resolution 2.10 Å R-free 0.211
1KEE Inactivation of the Amidotransferase Activity of Carbamoyl Phosphate Synthetase by the Antibiotic Acivicin Deposited 2001-11-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 1–382（382 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 5 PO4 PHOSPHATE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions batch；pH 7.4；277 K；PEG 8000, Hepes, potassium chloride, manganese chloride, ornithine, tetraethylammonium chloride, HEPPS, pH 7.4, batch, temperature 277K	Resolution 2.10 Å R-free 0.211
1KEE Inactivation of the Amidotransferase Activity of Carbamoyl Phosphate Synthetase by the Antibiotic Acivicin Deposited 2001-11-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–382（382 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 6 PO4 PHOSPHATE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions batch；pH 7.4；277 K；PEG 8000, Hepes, potassium chloride, manganese chloride, ornithine, tetraethylammonium chloride, HEPPS, pH 7.4, batch, temperature 277K	Resolution 2.10 Å R-free 0.211
1KEE Inactivation of the Amidotransferase Activity of Carbamoyl Phosphate Synthetase by the Antibiotic Acivicin Deposited 2001-11-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–382（382 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	MN MANGANESE (II) ION × 3 K POTASSIUM ION × 8 CL CHLORIDE ION × 6 PO4 PHOSPHATE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ORN L-ornithine × 1 NET TETRAETHYLAMMONIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions batch；pH 7.4；277 K；PEG 8000, Hepes, potassium chloride, manganese chloride, ornithine, tetraethylammonium chloride, HEPPS, pH 7.4, batch, temperature 277K	Resolution 2.10 Å R-free 0.211
1M6V Crystal Structure of the G359F (small subunit) Point Mutant of Carbamoyl Phosphate Synthetase Deposited 2002-07-17	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain B 1–382（382 aa） Chain D 1–382（382 aa） Chain F 1–382（382 aa） Chain H 1–382（382 aa）	Mutation：G359F Mutation：G359F Mutation：G359F Mutation：G359F	MN MANGANESE (II) ION × 12 K POTASSIUM ION × 26 CL CHLORIDE ION × 28 PO4 PHOSPHATE ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 8 ORN L-ornithine × 4 NET TETRAETHYLAMMONIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions batch；pH 7.4；277 K；PEG-8000, manganese chloride, potassium chloride, ADP, ornithine, tetraethylammonium chloride, HEPPS, pH 7.4, batch, temperature 277K	Resolution 2.10 Å R-free 0.245
1T36 Crystal structure of E. coli carbamoyl phosphate synthetase small subunit mutant C248D complexed with uridine 5'-monophosphate Deposited 2004-04-24	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain B 1–382（382 aa） Chain D 1–382（382 aa） Chain F 1–382（382 aa） Chain H 1–382（382 aa）	Mutation：C248D Mutation：C248D Mutation：C248D Mutation：C248D	MN MANGANESE (II) ION × 12 K POTASSIUM ION × 22 PO4 PHOSPHATE ION × 5 CL CHLORIDE ION × 27 ADP ADENOSINE-5'-DIPHOSPHATE × 8 ORN L-ornithine × 4 NET TETRAETHYLAMMONIUM ION × 4 U5P URIDINE-5'-MONOPHOSPHATE × 4	X-RAY DIFFRACTION X-ray crystallization conditions batch；pH 7.4；277 K；PEG 8000, tetramethylammonium chloride, potassium chloride, manganese chloride, ornithine, ADP, HEPES, pH 7.4, batch, temperature 277K	Resolution 2.10 Å R-free 0.209

7 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CARA_ECOLI
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–382； UniProt 1–382 Author chain D； PDBConstruct 1–382； UniProt 1–382 Author chain F； PDBConstruct 1–382； UniProt 1–382 Author chain H； PDBConstruct 1–382； UniProt 1–382

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	1c3o
Deposition date deposition_date	1999-07-28
Structure title title	CRYSTAL STRUCTURE OF THE CARBAMOYL PHOSPHATE SYNTHETASE: SMALL SUBUNIT MUTANT C269S WITH BOUND GLUTAMINE
Keywords keywords	AMIDOTRANSFERASE, MICHAELIS COMPLEX, ATP-GRASP, LIGASE; LIGASE
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	72.27 Å
Radius of gyration Rg (electron density) rg_electron	72.33 Å
Forward intensity I(0) i0	5743040000.00
Molecular weight molecular_weight	637940.0 kDa
Excluded volume excluded_volume	796150 Å³
Envelope volume envelope_volume	1151700 Å³
Hydration-shell volume shell_volume	131860 Å³
Envelope diameter envelope_diameter	240.2 Å
Shell Rg shell_rg	75.48 Å
Envelope Rg envelope_rg	68.84 Å
Shape Rg shape_rg	72.36 Å
Total Rg total_rg	72.25 Å
Total atoms total_atoms	44673
Residues n_residues	5748
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	251.2 Å
Rg (real space) rg_real	72.32 Å
Rg uncertainty (real space) rg_real_error	2.89 Å
I(0) (real space) i0_real	5.7430e+09
I(0) uncertainty (real space) i0_real_error	1.3360e+08
Rg (reciprocal space) rg_reciprocal	71.92 Å
I(0) (reciprocal space) i0_reciprocal	5738000000.0000
Solution quality estimate total_estimate	0.8527
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	91.3 Å
Skewness Skewness skewness	0.243
Kurtosis Kurtosis kurtosis	-0.580
Angular range angular_range	— – 0.1100 Å⁻¹
Current regularization parameter α current_alpha	0.0002
Highest regularization parameter α highest_alpha	195200000.0000
Real-space data points n_real_points	23
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.835; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.577

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (11)

Entity 1 Entity 1 polymer

Description description	CARBAMOYL PHOSPHATE SYNTHETASE: LARGE SUBUNIT
Molecular weight formula_weight	117981.8 kDa
EC 编号 ec_number	6.3.5.5
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C,E,G
Atom count atom_count	48477

MPKRTDIKSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPIHWEVVRKIIEKERPDAVLPTMGGQTALNCALELERQGVLEEFGVTMIGATADAIDKAEDRRRFDVAMKKIGLETARSGIAHTMEEALAVAADVGFPCIIRPSFTMGGSGGGIAYNREEFEEICARGLDLSPTKELLIDESLIGWKEYEMEVVRDKNDNCIIVCSIENFDAMGIHTGDSITVAPAQTLTDKEYQIMRNASMAVLREIGVETGGSNVQFAVNPKNGRLIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLDELMNDITGGRTPASFEPSIDYVVTKIPRFNFEKFAGANDRLTTQMKSVGEVMAIGRTQQESLQKALRGLEVGATGFDPKVSLDDPEALTKIRRELKDAGADRIWYIADAFRAGLSVDGVFNLTNIDRWFLVQIEELVRLEEKVAEVGITGLNADFLRQLKRKGFADARLAKLAGVREAEIRKLRDQYDLHPVYKRVDTCAAEFATDTAYMYSTYEEECEANPSTDREKIMVLGGGPNRIGQGIEFDYCCVHASLALREDGYETIMVNCNPETVSTDYDTSDRLYFEPVTLEDVLEIVRIEKPKGVIVQYGGQTPLKLARALEAAGVPVIGTSPDAIDRAEDRERFQHAVERLKLKQPANATVTAIEMAVEKAKEIGYPLVVRPSYVLGGRAMEIVYDEADLRRYFQTAVSVSNDAPVLLDHFLDDAVEVDVDAICDGEMVLIGGIMEHIEQAGVHSGDSACSLPAYTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAVKNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAARVMAGKSLAEQGVTKEVIPPYYSVKEVVLPFNKFPGVDPLLGPEMRSTGEVMGVGRTFAEAFAKAQLGSNSTMKKHGRALLSVREGDKERVVDLAAKLLKQGFELDATHGTAIVLGEAGINPRLVNKVHEGRPHIQDRIKNGEYTYIINTTSGRRAIEDSRVIRRSALQYKVHYDTTLNGGFATAMALNADATEKVISVQEMHAQIK

来源 Source

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	562
宿主生物 host_organism	Bacteria

Entity 2 Entity 2 polymer

Description description	CARBAMOYL PHOSPHATE SYNTHETASE: SMALL SUBUNIT
Molecular weight formula_weight	41465.8 kDa
EC 编号 ec_number	6.3.5.5
Mutation mutation	C269S
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D,F,H

MIKSALLVLEDGTQFHGRAIGATGSAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNDADEESSQVHAQGLVIRDLPLIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCIIAGDNPDAALALEKARAFPGLNGMDLAKEVTTAEAYSWTQGSWTLTGGLPEAKKEDELPFHVVAYDFGAKRNILRMLVDRGCRLTIVPAQTSAEDVLKMNPDGIFLSNGPGDPAPCDYAITAIQKFLETDIPVFGISLGHQLLALASGAKTVKMKFGHHGGNHPVKDVEKNVVMITAQNHGFAVDEATLPANLRVTHKSLFDGTLQGIHRTDKPAFSFQGHPEASPGPHDAAPLFDHFIELIEQYRKTAK

来源 Source

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	562
宿主生物 host_organism	Bacteria

Entity 3 Entity 3 non-polymer

Description description	MANGANESE (II) ION
Molecular weight formula_weight	54.9 kDa
Source method src_method	syn
Copy count entity_count	12

Entity 4 Entity 4 non-polymer

Description description	POTASSIUM ION
Molecular weight formula_weight	39.1 kDa
Source method src_method	syn
Copy count entity_count	32

Entity 5 Entity 5 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	16

Entity 6 Entity 6 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	5

Entity 7 Entity 7 non-polymer

Description description	ADENOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	427.2 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 8 Entity 8 non-polymer

Description description	L-ornithine
Molecular weight formula_weight	132.2 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 9 Entity 9 non-polymer

Description description	GLUTAMINE
Molecular weight formula_weight	146.1 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 10 Entity 10 non-polymer

Description description	TETRAETHYLAMMONIUM ION
Molecular weight formula_weight	130.3 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 11 Entity 11 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	3666

▼

7. Fold Classification (SCOP + CATH) 72 domains

SCOP 2.08 (32 domains)

Domain ID domain_id	d1c3oa1
Class class	a — All alpha proteins
Fold Fold fold	a.92 — Carbamoyl phosphate synthetase, large subunit connection domain
Superfamily Superfamily superfamily	a.92.1 — Carbamoyl phosphate synthetase, large subunit connection domain
Family Family family	a.92.1.1 — Carbamoyl phosphate synthetase, large subunit connection domain

Domain ID domain_id	d1c3oa2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.24 — Methylglyoxal synthase-like
Superfamily Superfamily superfamily	c.24.1 — Methylglyoxal synthase-like
Family Family family	c.24.1.1 — Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain

Domain ID domain_id	d1c3oa3
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.30 — PreATP-grasp domain
Superfamily Superfamily superfamily	c.30.1 — PreATP-grasp domain
Family Family family	c.30.1.1 — BC N-terminal domain-like

Domain ID domain_id	d1c3oa4
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.30 — PreATP-grasp domain
Superfamily Superfamily superfamily	c.30.1 — PreATP-grasp domain
Family Family family	c.30.1.1 — BC N-terminal domain-like

Domain ID domain_id	d1c3oa5
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.142 — ATP-grasp
Superfamily Superfamily superfamily	d.142.1 — Glutathione synthetase ATP-binding domain-like
Family Family family	d.142.1.2 — BC ATP-binding domain-like

Domain ID domain_id	d1c3oa6
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.142 — ATP-grasp
Superfamily Superfamily superfamily	d.142.1 — Glutathione synthetase ATP-binding domain-like
Family Family family	d.142.1.2 — BC ATP-binding domain-like

Domain ID domain_id	d1c3ob1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.8 — The 'swivelling' beta/beta/alpha domain
Superfamily Superfamily superfamily	c.8.3 — Carbamoyl phosphate synthetase, small subunit N-terminal domain
Family Family family	c.8.3.1 — Carbamoyl phosphate synthetase, small subunit N-terminal domain

Domain ID domain_id	d1c3ob2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.23 — Flavodoxin-like
Superfamily Superfamily superfamily	c.23.16 — Class I glutamine amidotransferase-like
Family Family family	c.23.16.1 — Class I glutamine amidotransferases (GAT)

Domain ID domain_id	d1c3oc1
Class class	a — All alpha proteins
Fold Fold fold	a.92 — Carbamoyl phosphate synthetase, large subunit connection domain
Superfamily Superfamily superfamily	a.92.1 — Carbamoyl phosphate synthetase, large subunit connection domain
Family Family family	a.92.1.1 — Carbamoyl phosphate synthetase, large subunit connection domain

Domain ID domain_id	d1c3oc2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.24 — Methylglyoxal synthase-like
Superfamily Superfamily superfamily	c.24.1 — Methylglyoxal synthase-like
Family Family family	c.24.1.1 — Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain

Domain ID domain_id	d1c3oc3
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.30 — PreATP-grasp domain
Superfamily Superfamily superfamily	c.30.1 — PreATP-grasp domain
Family Family family	c.30.1.1 — BC N-terminal domain-like

Domain ID domain_id	d1c3oc4
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.30 — PreATP-grasp domain
Superfamily Superfamily superfamily	c.30.1 — PreATP-grasp domain
Family Family family	c.30.1.1 — BC N-terminal domain-like

Domain ID domain_id	d1c3oc5
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.142 — ATP-grasp
Superfamily Superfamily superfamily	d.142.1 — Glutathione synthetase ATP-binding domain-like
Family Family family	d.142.1.2 — BC ATP-binding domain-like

Domain ID domain_id	d1c3oc6
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.142 — ATP-grasp
Superfamily Superfamily superfamily	d.142.1 — Glutathione synthetase ATP-binding domain-like
Family Family family	d.142.1.2 — BC ATP-binding domain-like

Domain ID domain_id	d1c3od1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.8 — The 'swivelling' beta/beta/alpha domain
Superfamily Superfamily superfamily	c.8.3 — Carbamoyl phosphate synthetase, small subunit N-terminal domain
Family Family family	c.8.3.1 — Carbamoyl phosphate synthetase, small subunit N-terminal domain

Domain ID domain_id	d1c3od2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.23 — Flavodoxin-like
Superfamily Superfamily superfamily	c.23.16 — Class I glutamine amidotransferase-like
Family Family family	c.23.16.1 — Class I glutamine amidotransferases (GAT)

Domain ID domain_id	d1c3oe1
Class class	a — All alpha proteins
Fold Fold fold	a.92 — Carbamoyl phosphate synthetase, large subunit connection domain
Superfamily Superfamily superfamily	a.92.1 — Carbamoyl phosphate synthetase, large subunit connection domain
Family Family family	a.92.1.1 — Carbamoyl phosphate synthetase, large subunit connection domain

Domain ID domain_id	d1c3oe2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.24 — Methylglyoxal synthase-like
Superfamily Superfamily superfamily	c.24.1 — Methylglyoxal synthase-like
Family Family family	c.24.1.1 — Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain

Domain ID domain_id	d1c3oe3
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.30 — PreATP-grasp domain
Superfamily Superfamily superfamily	c.30.1 — PreATP-grasp domain
Family Family family	c.30.1.1 — BC N-terminal domain-like

Domain ID domain_id	d1c3oe4
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.30 — PreATP-grasp domain
Superfamily Superfamily superfamily	c.30.1 — PreATP-grasp domain
Family Family family	c.30.1.1 — BC N-terminal domain-like

Domain ID domain_id	d1c3oe5
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.142 — ATP-grasp
Superfamily Superfamily superfamily	d.142.1 — Glutathione synthetase ATP-binding domain-like
Family Family family	d.142.1.2 — BC ATP-binding domain-like

Domain ID domain_id	d1c3oe6
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.142 — ATP-grasp
Superfamily Superfamily superfamily	d.142.1 — Glutathione synthetase ATP-binding domain-like
Family Family family	d.142.1.2 — BC ATP-binding domain-like

Domain ID domain_id	d1c3of1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.8 — The 'swivelling' beta/beta/alpha domain
Superfamily Superfamily superfamily	c.8.3 — Carbamoyl phosphate synthetase, small subunit N-terminal domain
Family Family family	c.8.3.1 — Carbamoyl phosphate synthetase, small subunit N-terminal domain

Domain ID domain_id	d1c3of2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.23 — Flavodoxin-like
Superfamily Superfamily superfamily	c.23.16 — Class I glutamine amidotransferase-like
Family Family family	c.23.16.1 — Class I glutamine amidotransferases (GAT)

Domain ID domain_id	d1c3og1
Class class	a — All alpha proteins
Fold Fold fold	a.92 — Carbamoyl phosphate synthetase, large subunit connection domain
Superfamily Superfamily superfamily	a.92.1 — Carbamoyl phosphate synthetase, large subunit connection domain
Family Family family	a.92.1.1 — Carbamoyl phosphate synthetase, large subunit connection domain

Domain ID domain_id	d1c3og2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.24 — Methylglyoxal synthase-like
Superfamily Superfamily superfamily	c.24.1 — Methylglyoxal synthase-like
Family Family family	c.24.1.1 — Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain

Domain ID domain_id	d1c3og3
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.30 — PreATP-grasp domain
Superfamily Superfamily superfamily	c.30.1 — PreATP-grasp domain
Family Family family	c.30.1.1 — BC N-terminal domain-like

Domain ID domain_id	d1c3og4
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.30 — PreATP-grasp domain
Superfamily Superfamily superfamily	c.30.1 — PreATP-grasp domain
Family Family family	c.30.1.1 — BC N-terminal domain-like

Domain ID domain_id	d1c3og5
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.142 — ATP-grasp
Superfamily Superfamily superfamily	d.142.1 — Glutathione synthetase ATP-binding domain-like
Family Family family	d.142.1.2 — BC ATP-binding domain-like

Domain ID domain_id	d1c3og6
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.142 — ATP-grasp
Superfamily Superfamily superfamily	d.142.1 — Glutathione synthetase ATP-binding domain-like
Family Family family	d.142.1.2 — BC ATP-binding domain-like

Domain ID domain_id	d1c3oh1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.8 — The 'swivelling' beta/beta/alpha domain
Superfamily Superfamily superfamily	c.8.3 — Carbamoyl phosphate synthetase, small subunit N-terminal domain
Family Family family	c.8.3.1 — Carbamoyl phosphate synthetase, small subunit N-terminal domain

Domain ID domain_id	d1c3oh2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.23 — Flavodoxin-like
Superfamily Superfamily superfamily	c.23.16 — Class I glutamine amidotransferase-like
Family Family family	c.23.16.1 — Class I glutamine amidotransferases (GAT)

CATH v4.4 (40 domains)

Domain ID domain_id	1c3oA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1c3oA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	470 — D-amino Acid Aminotransferase; Chain A, domain 1
Homologous superfamily homologous superfamily	20 — ATP-grasp fold, B domain

Domain ID domain_id	1c3oA03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1490 — Dna Ligase; domain 1
Homologous superfamily homologous superfamily	20 — ATP-grasp fold, A domain

Domain ID domain_id	1c3oA04
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1030 — Carbamoyl Phosphate Synthetase; Chain A, domain 4
Homologous superfamily homologous superfamily	10 — Carbamoyl-phosphate synthetase, large subunit oligomerisation domain

Domain ID domain_id	1c3oA05
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1c3oA06
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	470 — D-amino Acid Aminotransferase; Chain A, domain 1
Homologous superfamily homologous superfamily	20 — ATP-grasp fold, B domain

Domain ID domain_id	1c3oA07
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1490 — Dna Ligase; domain 1
Homologous superfamily homologous superfamily	20 — ATP-grasp fold, A domain

Domain ID domain_id	1c3oA08
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1380 — Methylglyoxal synthase-like domain

Domain ID domain_id	1c3oB01
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	30 — Glucose Oxidase; domain 1
Homologous superfamily homologous superfamily	20 — Carbamoyl-phosphate synthase small subunit, N-terminal domain

Domain ID domain_id	1c3oB02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	880 — Class I glutamine amidotransferase (GATase) domain

Domain ID domain_id	1c3oC01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1c3oC02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	470 — D-amino Acid Aminotransferase; Chain A, domain 1
Homologous superfamily homologous superfamily	20 — ATP-grasp fold, B domain

Domain ID domain_id	1c3oC03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1490 — Dna Ligase; domain 1
Homologous superfamily homologous superfamily	20 — ATP-grasp fold, A domain

Domain ID domain_id	1c3oC04
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1030 — Carbamoyl Phosphate Synthetase; Chain A, domain 4
Homologous superfamily homologous superfamily	10 — Carbamoyl-phosphate synthetase, large subunit oligomerisation domain

Domain ID domain_id	1c3oC05
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1c3oC06
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	470 — D-amino Acid Aminotransferase; Chain A, domain 1
Homologous superfamily homologous superfamily	20 — ATP-grasp fold, B domain

Domain ID domain_id	1c3oC07
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1490 — Dna Ligase; domain 1
Homologous superfamily homologous superfamily	20 — ATP-grasp fold, A domain

Domain ID domain_id	1c3oC08
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1380 — Methylglyoxal synthase-like domain

Domain ID domain_id	1c3oD01
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	30 — Glucose Oxidase; domain 1
Homologous superfamily homologous superfamily	20 — Carbamoyl-phosphate synthase small subunit, N-terminal domain

Domain ID domain_id	1c3oD02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	880 — Class I glutamine amidotransferase (GATase) domain

Domain ID domain_id	1c3oE01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1c3oE02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	470 — D-amino Acid Aminotransferase; Chain A, domain 1
Homologous superfamily homologous superfamily	20 — ATP-grasp fold, B domain

Domain ID domain_id	1c3oE03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1490 — Dna Ligase; domain 1
Homologous superfamily homologous superfamily	20 — ATP-grasp fold, A domain

Domain ID domain_id	1c3oE04
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1030 — Carbamoyl Phosphate Synthetase; Chain A, domain 4
Homologous superfamily homologous superfamily	10 — Carbamoyl-phosphate synthetase, large subunit oligomerisation domain

Domain ID domain_id	1c3oE05
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1c3oE06
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	470 — D-amino Acid Aminotransferase; Chain A, domain 1
Homologous superfamily homologous superfamily	20 — ATP-grasp fold, B domain

Domain ID domain_id	1c3oE07
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1490 — Dna Ligase; domain 1
Homologous superfamily homologous superfamily	20 — ATP-grasp fold, A domain

Domain ID domain_id	1c3oE08
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1380 — Methylglyoxal synthase-like domain

Domain ID domain_id	1c3oF01
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	30 — Glucose Oxidase; domain 1
Homologous superfamily homologous superfamily	20 — Carbamoyl-phosphate synthase small subunit, N-terminal domain

Domain ID domain_id	1c3oF02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	880 — Class I glutamine amidotransferase (GATase) domain

Domain ID domain_id	1c3oG01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1c3oG02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	470 — D-amino Acid Aminotransferase; Chain A, domain 1
Homologous superfamily homologous superfamily	20 — ATP-grasp fold, B domain

Domain ID domain_id	1c3oG03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1490 — Dna Ligase; domain 1
Homologous superfamily homologous superfamily	20 — ATP-grasp fold, A domain

Domain ID domain_id	1c3oG04
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1030 — Carbamoyl Phosphate Synthetase; Chain A, domain 4
Homologous superfamily homologous superfamily	10 — Carbamoyl-phosphate synthetase, large subunit oligomerisation domain

Domain ID domain_id	1c3oG05
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1c3oG06
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	470 — D-amino Acid Aminotransferase; Chain A, domain 1
Homologous superfamily homologous superfamily	20 — ATP-grasp fold, B domain

Domain ID domain_id	1c3oG07
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1490 — Dna Ligase; domain 1
Homologous superfamily homologous superfamily	20 — ATP-grasp fold, A domain

Domain ID domain_id	1c3oG08
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1380 — Methylglyoxal synthase-like domain

Domain ID domain_id	1c3oH01
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	30 — Glucose Oxidase; domain 1
Homologous superfamily homologous superfamily	20 — Carbamoyl-phosphate synthase small subunit, N-terminal domain

Domain ID domain_id	1c3oH02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	880 — Class I glutamine amidotransferase (GATase) domain

▶

8. Citations (1)

▶

Unit-cell length a length_a	152.500 Å
Unit-cell length b length_b	164.400 Å
Unit-cell length c length_c	332.600 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	16

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.100 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.1890
R_work r_work	0.1880
R_free r_free	0.2580

fit	/app/data/saxs_computation/c3/1c3o/1c3o.fit
pddf	/app/data/pr_computation/c3/1c3o/1c3o.pr.out
profile	/app/data/saxs_computation/c3/1c3o/1c3o.dat

CRYSTAL STRUCTURE OF THE CARBAMOYL PHOSPHATE SYNTHETASE: SMALL SUBUNIT MUTANT C269S WITH BOUND GLUTAMINE

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

CARBAMOYL PHOSPHATE SYNTHETASE: LARGE SUBUNIT

State in the Current Structure

Other States of the Same Protein in the Database

CARBAMOYL PHOSPHATE SYNTHETASE: SMALL SUBUNIT

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

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (11)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 non-polymer

Entity 9 Entity 9 non-polymer

Entity 10 Entity 10 non-polymer

Entity 11 Entity 11 water

7. Fold Classification (SCOP + CATH) 72 domains

SCOP 2.08 (32 domains)

CATH v4.4 (40 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)