1ekx

THE ISOLATED, UNREGULATED CATALYTIC TRIMER OF ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH BISUBSTRATE ANALOG PALA (N-(PHOSPHONACETYL)-L-ASPARTATE)

Method: X-RAY DIFFRACTION D_max: 97.9 Å Quality: EXCELLENT

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

ASPARTATE TRANSCARBAMOYLASE

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 homooligomer Homooligomer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 1–311 Chain B； UniProt 1–311 Chain C； UniProt 1–311	Fragment：CATALYTIC SUBUNIT	PAL N-(PHOSPHONACETYL)-L-ASPARTIC ACID × 3 CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；Calcium Acetate, PEG 8000, tris-HCL, 2-mercaptoethanol, PALA, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.95 Å R-free 0.214

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 1EKX	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1ACM ARGININE 54 IN THE ACTIVE SITE OF ESCHERICHIA COLI ASPARTATE TRANSCARBAMOYLASE IS CRITICAL FOR CATALYSIS: A SITE-SPECIFIC MUTAGENESIS, NMR AND X-RAY CRYSTALLOGRAPHY STUDY Deposited 1992-07-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Not recorded	PAL N-(PHOSPHONACETYL)-L-ASPARTIC ACID × 6 ZN ZINC ION × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å
1AT1 CRYSTAL STRUCTURES OF PHOSPHONOACETAMIDE LIGATED T AND PHOSPHONOACETAMIDE AND MALONATE LIGATED R STATES OF ASPARTATE CARBAMOYLTRANSFERASE AT 2.8-ANGSTROMS RESOLUTION AND NEUTRAL P*H Deposited 1989-09-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Not recorded	MLI MALONATE ION × 6 PCT PHOSPHONOACETAMIDE × 6 ZN ZINC ION × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å
1D09 ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH N-PHOSPHONACETYL-L-ASPARTATE (PALA) Deposited 1999-09-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 2–311（310 aa） Chain C 2–311（310 aa）	Not recorded	PAL N-(PHOSPHONACETYL)-L-ASPARTIC ACID × 6 ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions LIQUID DIFFUSION；pH 5.9；ENZYME: 12 MG/ML; BUFFER: 50 MM MALEIC ACID, 3 MM SOLDIUM AZIDE 1 MM N- PHOSPHONACETYL-L-ASPARTATE, pH 5.9, LIQUID DIFFUSION	Resolution 2.10 Å R-free 0.234
1EZZ CRYSTAL STRUCTURE OF E. COLI ASPARTATE TRANSCARBAMOYLASE P268A MUTANT IN THE T-STATE Deposited 2000-05-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Mutation：P268A Mutation：P268A	ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；ENZYME: 24 mg/ml; 1:1 enzyme to-buffer ratio, BUFFER: 20 mm HEPES, 14% (w/v) PEG 1450, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K	Resolution 2.70 Å R-free 0.242
1F1B CRYSTAL STRUCTURE OF E. COLI ASPARTATE TRANSCARBAMOYLASE P268A MUTANT IN THE R-STATE IN THE PRESENCE OF N-PHOSPHONACETYL-L-ASPARTATE Deposited 2000-05-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Mutation：P268A Mutation：P268A	PAL N-(PHOSPHONACETYL)-L-ASPARTIC ACID × 6 ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions MICRODIALYSIS；pH 5.75；293 K；ENZYME: 7.5 mg/ml in 50 uL microdialysis button. BUFFER: 20 mm maleic acid, 3 mM sodium azide, 1 mM N-phosphonacetyl-L-aspartate, pH 5.75, MICRODIALYSIS, temperature 293K	Resolution 2.30 Å R-free 0.232
1I5O CRYSTAL STRUCTURE OF MUTANT R105A OF E. COLI ASPARTATE TRANSCARBAMOYLASE Deposited 2001-02-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Mutation：R105A Mutation：R105A	ZN ZINC ION × 6 PAL N-(PHOSPHONACETYL)-L-ASPARTIC ACID × 3	X-RAY DIFFRACTION X-ray crystallization conditions MICRODIALYSIS；pH 5.7；293 K；Tris buffer, maleic acid, pH 5.7, MICRODIALYSIS, temperature 293K	Resolution 2.80 Å R-free 0.212
1NBE ASPARTATE TRANSCARBAMOYLASE REGULATORY CHAIN MUTANT (T82A) Deposited 1998-04-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Mutation：T82A Mutation：T82A	MLT D-MALATE × 12 ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.85；7.5 MG/ML PROTEIN DIALYZED AGAINST 100MM MALIC ACID AT PH 5.85,	Resolution 2.60 Å R-free 0.237
1Q95 Aspartate Transcarbamylase (ATCase) of Escherichia coli: A New Crystalline R State Bound to PALA, or to Product Analogues Phosphate and Citrate Deposited 2003-08-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain B 1–310（310 aa） Chain C 1–310（310 aa） Chain D 1–310（310 aa） Chain E 1–310（310 aa） Chain F 1–310（310 aa）	Not recorded	PAL N-(PHOSPHONACETYL)-L-ASPARTIC ACID × 6 ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；294 K；PEG-mmes 2000, lithium sulfate, sodium azide, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.46 Å R-free 0.270
1R0B Aspartate Transcarbamylase (ATCase) of Escherichia coli: A New Crystalline R State Bound to PALA, or to Product Analogues Phosphate and Citrate Deposited 2003-09-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain B 1–310（310 aa） Chain C 1–310（310 aa） Chain D 1–310（310 aa） Chain E 1–310（310 aa） Chain F 1–310（310 aa）	Not recorded	FLC CITRATE ANION × 6 PO4 PHOSPHATE ION × 6 ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions MICRODIALYSIS；pH 5.8；294 K；sodium citrate, sodium phosphate, N-ethylmorpholine, pH 5.8, MICRODIALYSIS, temperature 294K	Resolution 2.90 Å R-free 0.300
1R0C Products in the T State of Aspartate Transcarbamylase: Crystal Structure of the Phosphate and N-carbamyl-L-aspartate Ligated Enzyme Deposited 2003-09-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain G 1–310（310 aa）	Not recorded	PO4 PHOSPHATE ION × 6 NCD N-CARBAMOYL-L-ASPARTATE × 6 ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；PEG 4000, Hepes-Na, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.37 Å R-free 0.274
1RAA CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY Deposited 1992-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 2–311（310 aa） Chain C 2–311（310 aa）	Not recorded	ZN ZINC ION × 6 CTP CYTIDINE-5'-TRIPHOSPHATE × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
1RAB CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY Deposited 1992-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 2–311（310 aa） Chain C 2–311（310 aa）	Not recorded	ZN ZINC ION × 6 CTP CYTIDINE-5'-TRIPHOSPHATE × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
1RAC CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY Deposited 1992-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 2–311（310 aa） Chain C 2–311（310 aa）	Not recorded	ZN ZINC ION × 6 CTP CYTIDINE-5'-TRIPHOSPHATE × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
1RAD CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY Deposited 1992-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 2–311（310 aa） Chain C 2–311（310 aa）	Not recorded	ZN ZINC ION × 6 CTP CYTIDINE-5'-TRIPHOSPHATE × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
1RAE CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY Deposited 1992-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 2–311（310 aa） Chain C 2–311（310 aa）	Not recorded	ZN ZINC ION × 6 CTP CYTIDINE-5'-TRIPHOSPHATE × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
1RAF CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY Deposited 1992-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 2–311（310 aa） Chain C 2–311（310 aa）	Not recorded	ZN ZINC ION × 6 CTP CYTIDINE-5'-TRIPHOSPHATE × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
1RAG CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY Deposited 1992-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 2–311（310 aa） Chain C 2–311（310 aa）	Not recorded	ZN ZINC ION × 6 CTP CYTIDINE-5'-TRIPHOSPHATE × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
1RAH CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY Deposited 1992-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 2–311（310 aa） Chain C 2–311（310 aa）	Not recorded	ZN ZINC ION × 6 CTP CYTIDINE-5'-TRIPHOSPHATE × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
1RAI CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY Deposited 1992-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 2–311（310 aa） Chain C 2–311（310 aa）	Not recorded	ZN ZINC ION × 6 CTP CYTIDINE-5'-TRIPHOSPHATE × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
1SKU E. coli Aspartate Transcarbamylase 240's Loop Mutant (K244N) Deposited 2004-03-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Mutation：K244N Mutation：K244N	MLI MALONATE ION × 6 ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；Prior to crystallization the enzyme was dialyzed into 40 mM KH2PO4, 2.0 mM 2-mercaptoethanol, 0.2 mM EDTA, pH 7.0 for 24 hours. Single crystals of the K244N mutant were obtained by mixing a 20 mg/ml filtered solution (0.22 m) of the K244N enzyme with a solution of 17% (w/v) PEG 1450, 50 mM malonate, 0.2 mM EDTA, 1 mM sodium azide and 20 mM Bis-Tris buffer pH 7.0 in a 1:1 ratio (v/v), VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.60 Å R-free 0.231
1TTH Aspartate Transcarbamoylase Catalytic Chain Mutant Glu50Ala Complexed with N-(Phosphonacetyl-L-Aspartate) (PALA) Deposited 2004-06-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Mutation：E50A Mutation：E50A	PAL N-(PHOSPHONACETYL)-L-ASPARTIC ACID × 6 ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.9；295 K；50 mM maleic-acid-N-ethyl-morpholine buffer (pH 5.84) containing 3 mM sodium azide and 1 mM PALA, pH 5.90, MICRODIALYSIS, temperature 295K	Resolution 2.80 Å R-free 0.264
1TU0 Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide Deposited 2004-06-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Mutation：E50A Mutation：E50A	PCT PHOSPHONOACETAMIDE × 6 ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；295 K；The Glu50Ala mutant was crystallized in 100 mM sodium citrate, 1 mM 2-mercaptoethanol, and 15% PEG 8000 pH 7.0. Before mounting, 50 mM PAM was added and the crystal soaked, pH 6.0, MICRODIALYSIS, temperature 295K, pH 6.00	Resolution 2.55 Å R-free 0.279
1TUG Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide, Malonate, and Cytidine-5-Prime-Triphosphate (CTP) Deposited 2004-06-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Mutation：E50A Mutation：E50A	MLI MALONATE ION × 6 PCT PHOSPHONOACETAMIDE × 6 ZN ZINC ION × 6 CTP CYTIDINE-5'-TRIPHOSPHATE × 6	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；295 K；100 mM sodium citrate, 1 mM 2-mercaptoethanol, 0.2 mM EDTA and 1.0 mM CTP pH 6.0 then soaked for 24 hours in 100 mM malonate, 2 mM CTP, 3 mM sodium azide, 2 mM 2-mercaptoethanol, and 15% PEG 8000 pH 7.0. Before mounting, 50 mM PAM was added and the crystal allowed to soak until data collected., MICRODIALYSIS, temperature 295K, pH 6.00	Resolution 2.10 Å R-free 0.272
1XJW The Structure of E. coli Aspartate Transcarbamoylase Q137A Mutant in The R-State Deposited 2004-09-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Mutation：Q137A Mutation：Q137A	PAL N-(PHOSPHONACETYL)-L-ASPARTIC ACID × 6 ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions MICRODIALYSIS；pH 5.9；295 K；12 mg/ml Buffer 50 mM Maleic Acid, 3 mM Sodium Azide 1 mM N-Phosphonacetyl-L-Aspartate, pH 5.9, MICRODIALYSIS, temperature 295K	Resolution 2.71 Å R-free 0.223
2A0F Structure of D236A mutant E. coli Aspartate Transcarbamoylase in presence of Phosphonoacetamide at 2.90 A resolution Deposited 2005-06-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Mutation：D236A Mutation：D236A	PCT PHOSPHONOACETAMIDE × 3 ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions MICRODIALYSIS；pH 5.7；298 K；maleic acid, sodium azide, phosphonoacetamide, pH 5.7, MICRODIALYSIS, temperature 298K	Resolution 2.90 Å R-free 0.279
2AIR T-state Active Site of Aspartate Transcarbamylase:Crystal Structure of the Carbamyl Phosphate and L-alanosine Ligated Enzyme Deposited 2005-07-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain G 1–310（310 aa）	Not recorded	CP PHOSPHORIC ACID MONO(FORMAMIDE)ESTER × 6 AL0 3-[HYDROXY(NITROSO)AMINO]-L-ALANINE × 6 ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；PEG-4000, iso-propranol, sodium azide, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.00 Å R-free 0.273
2AT1 CRYSTAL STRUCTURES OF PHOSPHONOACETAMIDE LIGATED T AND PHOSPHONOACETAMIDE AND MALONATE LIGATED R STATES OF ASPARTATE CARBAMOYLTRANSFERASE AT 2.8-ANGSTROMS RESOLUTION AND NEUTRAL PH Deposited 1989-09-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Not recorded	PCT PHOSPHONOACETAMIDE × 6 ZN ZINC ION × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å
2ATC CRYSTAL AND MOLECULAR STRUCTURES OF NATIVE AND CTP-LIGANDED ASPARTATE CARBAMOYLTRANSFERASE FROM ESCHERICHIA COLI Deposited 1982-03-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa）	Not recorded	ZN ZINC ION × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.00 Å
2FZC The Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in Complex with Novel T State Inhibitors at 2.10 Resolution Deposited 2006-02-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Not recorded	EOP {ETHANE-1,2-DIYLBIS[IMINO(2-OXOETHANE-2,1-DIYL)]}BIS(PHOSPHONIC ACID) × 6 ZN ZINC ION × 6 CTP CYTIDINE-5'-TRIPHOSPHATE × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.7；298 K；ATCase holoenzyme was crystallized by microdialysis, using 50 L wells. The enzyme solution, at ~18 mg/mL, was dialyzed against a solution of 40 mM citric acid, 3 mM sodium azide, 1 mM 2-mercaptoethanol, 1 mM cytidine 5 -triphosphate, 0.2 mM EDTA (pH 5.7) , VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.10 Å R-free 0.250
2FZG The Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in Complex with Novel T State Inhibitors at 2.25 Resolution Deposited 2006-02-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Not recorded	EOB {1,3-PHENYLENEBIS[IMINO(2-OXOETHANE-2,1-DIYL)]}BIS(PHOSPHONIC ACID) × 6 ZN ZINC ION × 6 CTP CYTIDINE-5'-TRIPHOSPHATE × 6	X-RAY DIFFRACTION X-ray crystallization conditions MICRODIALYSIS；pH 5.7；298 K；ATCase holoenzyme was crystallized by microdialysis, using 50 L wells. The enzyme solution, at ~18 mg/mL, was dialyzed against a solution of 40 mM citric acid, 3 mM sodium azide, 1 mM 2-mercaptoethanol, 1 mM cytidine 5 -triphosphate, 0.2 mM EDTA (pH 5.7), MICRODIALYSIS, temperature 298K	Resolution 2.25 Å R-free 0.237
2FZK The Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in Complex with Novel T State Inhibitors at 2.50 Resolution Deposited 2006-02-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Not recorded	EOZ 3,5-BIS[(PHOSPHONOACETYL)AMINO]BENZOIC ACID × 6 ZN ZINC ION × 6 CTP CYTIDINE-5'-TRIPHOSPHATE × 6	X-RAY DIFFRACTION X-ray crystallization conditions MICRODIALYSIS；pH 5.7；298 K；ATCase holoenzyme was crystallized by microdialysis, using 50 L wells. The enzyme solution, at ~18 mg/mL, was dialyzed against a solution of 40 mM citric acid, 3 mM sodium azide, 1 mM 2-mercaptoethanol, 1 mM cytidine 5 -triphosphate, 0.2 mM EDTA (pH 5.7), MICRODIALYSIS, temperature 298K	Resolution 2.50 Å R-free 0.239
2H3E Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of N-phosphonacetyl-L-isoasparagine at 2.3A resolution Deposited 2006-05-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Not recorded	6PR (S)-4-AMINO-4-OXO-3-(2-PHOSPHONOACETAMIDO)BUTANOIC ACID × 6 ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions MICRODIALYSIS；pH 5.7；293 K；50 mM Maleic acid, 3 mM sodium azide, 1 mM N-phosphonacetyl-L-isoasparagine, pH 5.7, MICRODIALYSIS, temperature 293K	Resolution 2.30 Å R-free 0.250
2HSE Structure of D236A E. coli Aspartate Transcarbamoylase in the presence of phosphonoacetamide and l-Aspartate at 2.60 A resolution Deposited 2006-07-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Not recorded	PO4 PHOSPHATE ION × 3 PCT PHOSPHONOACETAMIDE × 6 ASP ASPARTIC ACID × 9 ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions MICRODIALYSIS；pH 5.8；293 K；50mM maleic acid, 3mM sodium azide, 10mM phosphonoacetamide, 20mM L-aspartate, pH 5.8, MICRODIALYSIS, temperature 293K	Resolution 2.60 Å R-free 0.254
2IPO E. coli Aspartate Transcarbamoylase complexed with N-phosphonacetyl-L-asparagine Deposited 2006-10-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Not recorded	1IP N~2~-(PHOSPHONOACETYL)-L-ASPARAGINE × 6 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 6 ZN ZINC ION × 6 MAE MALEIC ACID × 6	X-RAY DIFFRACTION X-ray crystallization conditions MICRODIALYSIS；pH 5.7；295 K；50 mM Maleic acid, 1 mM N-phosphonacetyl-L-asparagine, 3 mM Sodium Azide, pH 5.7, MICRODIALYSIS, temperature 295K	Resolution 2.60 Å R-free 0.253
2QG9 Structure of a regulatory subunit mutant D19A of ATCase from E. coli Deposited 2007-06-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 2–311（310 aa） Chain C 2–311（310 aa）	Not recorded	ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions MICRODIALYSIS；pH 5.7；298 K；0.1M citrate buffer, pH 5.7, MICRODIALYSIS, temperature 298.0K	Resolution 2.70 Å R-free 0.244
2QGF Structure of regulatory chain mutant H20A of asparate transcarbamoylase from E. coli Deposited 2007-06-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 2–311（310 aa） Chain C 2–311（310 aa）	Not recorded	ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions MICRODIALYSIS；pH 5.7；298 K；0.1M citric acid, pH 5.7, MICRODIALYSIS, temperature 298.0K	Resolution 2.20 Å R-free 0.223
3AT1 CRYSTAL STRUCTURES OF PHOSPHONOACETAMIDE LIGATED T AND PHOSPHONOACETAMIDE AND MALONATE LIGATED R STATES OF ASPARTATE CARBAMOYLTRANSFERASE AT 2.8-ANGSTROMS RESOLUTION AND NEUTRAL PH Deposited 1989-09-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Not recorded	PCT PHOSPHONOACETAMIDE × 6 ZN ZINC ION × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å
3CSU CATALYTIC TRIMER OF ESCHERICHIA COLI ASPARTATE TRANSCARBAMOYLASE Deposited 1999-04-22	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–310（310 aa） Fragment：CATALYTIC SUBUNIT Chain B 1–310（310 aa） Fragment：CATALYTIC SUBUNIT Chain C 1–310（310 aa） Fragment：CATALYTIC SUBUNIT	Not recorded	CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.8；pH 7.8	Resolution 1.88 Å R-free 0.291
3D7S Crystal structure of Wild-Type E. Coli Asparate Transcarbamoylase at pH 8.5 at 2.80 A Resolution Deposited 2008-05-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 2–311（310 aa） Chain C 2–311（310 aa）	Not recorded	ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；50 mM Tris 8K PEG, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.80 Å R-free 0.235
3MPU Crystal structure of the C47A/A241C disulfide-linked E. coli Aspartate Transcarbamoylase holoenzyme Deposited 2010-04-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 2–311（310 aa） Chain C 2–311（310 aa）	Mutation：C47A, A241C Mutation：C47A, A241C	PO4 PHOSPHATE ION × 12 ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions MICRODIALYSIS；pH 5.9；293 K；Protein at 10 mg/ml was dialyzed against solution containing 100 mM KH2PO4, 3mM NaN3, pH 5.9, MICRODIALYSIS, temperature 293K	Resolution 2.85 Å R-free 0.240
3MPU Crystal structure of the C47A/A241C disulfide-linked E. coli Aspartate Transcarbamoylase holoenzyme Deposited 2010-04-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain E 2–311（310 aa）	Mutation：C47A, A241C	PO4 PHOSPHATE ION × 12 ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions MICRODIALYSIS；pH 5.9；293 K；Protein at 10 mg/ml was dialyzed against solution containing 100 mM KH2PO4, 3mM NaN3, pH 5.9, MICRODIALYSIS, temperature 293K	Resolution 2.85 Å R-free 0.240
3NPM Crystal Structure of the C47A/A241C disulfide-linked C6 Aspartate Transcarbamoylase enzyme Deposited 2010-06-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 2–311（310 aa）	Mutation：A48C; C242A	PO4 PHOSPHATE ION × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；10 mg/mL of C47A/A241C c6 in 100 mM tris-acetate pH 8.3, in a 1:1 ratio (v/v), with reservoir. Crystallization buffer consisted of 40% PEG 1000, 100 mM NH4H2PO4, and 100 mM HEPES, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.10 Å R-free 0.205
4AT1 STRUCTURAL CONSEQUENCES OF EFFECTOR BINDING TO THE T STATE OF ASPARTATE CARBAMOYLTRANSFERASE. CRYSTAL STRUCTURES OF THE UNLIGATED AND ATP-, AND CTP-COMPLEXED ENZYMES AT 2.6-ANGSTROMS RESOLUTION Deposited 1990-04-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Not recorded	ZN ZINC ION × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.60 Å
4E2F Crystal Structure of E. coli Aspartate Transcarbamoylase K164E/E239K Mutant in an intermediate state Deposited 2012-03-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 2–311（310 aa） Chain C 2–311（310 aa） Chain E 2–311（310 aa） Chain G 2–311（310 aa） Chain I 2–311（310 aa） Chain K 2–311（310 aa）	Mutation：K164E, E239K Mutation：K164E, E239K Mutation：K164E, E239K Mutation：K164E, E239K Mutation：K164E, E239K Mutation：K164E, E239K	ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.75；293 K；16% (w/v) PEG 4000, 0.04 M Na2MoO4, 0.04 M N-cyclohexyl-3-aminopropanesulfonic acid, 30 mM Tris-acetate, pH 8.75, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.80 Å R-free 0.274
4F04 A Second Allosteric site in E. coli Aspartate Transcarbamoylase: R-state ATCase with UTP bound Deposited 2012-05-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 2–311（310 aa） Chain C 2–311（310 aa）	Not recorded	PAL N-(PHOSPHONACETYL)-L-ASPARTIC ACID × 6 ZN ZINC ION × 6 UTP URIDINE 5'-TRIPHOSPHATE × 6	X-RAY DIFFRACTION X-ray crystallization conditions MICRODIALYSIS；pH 5.95；298 K；50 mM maleic acid, 3 mM sodium azide, 1 mM PALA, adjusted to pH=5.95 with N-ethylmorpholine, MICRODIALYSIS, temperature 298K	Resolution 2.30 Å R-free 0.207
4FYV Aspartate Transcarbamoylase Complexed with dCTP Deposited 2012-07-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 2–311（310 aa） Chain C 2–311（310 aa）	Not recorded	PO4 PHOSPHATE ION × 3 ZN ZINC ION × 6 DCP 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE × 6	X-RAY DIFFRACTION X-ray crystallization conditions MICRODIALYSIS；pH 5.7；298 K；40 mM sodium citrate, 1 mM 2-mercaptoethanol, 0.2 mM EDTA, 1.0 mM dCTP, pH 5.7, MICRODIALYSIS, temperature 298K	Resolution 2.10 Å R-free 0.215
4FYW E. coli Aspartate Transcarbamoylase complexed with CTP Deposited 2012-07-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 2–311（310 aa） Chain C 2–311（310 aa）	Not recorded	ZN ZINC ION × 6 CTP CYTIDINE-5'-TRIPHOSPHATE × 6	X-RAY DIFFRACTION X-ray crystallization conditions MICRODIALYSIS；pH 5.7；298 K；40 mM sodium citrate, 1 mM 2-mercaptoethanol, 0.2 mM EDTA, 1.0 mM CTP, pH 5.7, MICRODIALYSIS, temperature 298K	Resolution 2.10 Å R-free 0.229
4FYX E. coli Aspartate Transcarbamoylase complexed with dCTP, UTP, and Mg2+ Deposited 2012-07-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 2–311（310 aa） Chain C 2–311（310 aa）	Not recorded	ZN ZINC ION × 6 UTP URIDINE 5'-TRIPHOSPHATE × 6 DCP 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions MICRODIALYSIS；pH 5.7；298 K；40 mM sodium citrate, 1 mM 2-mercaptoethanol, 0.2 mM EDTA, 1.0 mM dCTP, pH 5.7 (crystals soaked in 5 mM UTP and 5 mM Mg2+), MICRODIALYSIS, temperature 298K	Resolution 2.09 Å R-free 0.212
4FYY E. coli Aspartate Transcarbamoylase Complexed with CTP, UTP, and Mg2+ Deposited 2012-07-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 2–311（310 aa） Chain C 2–311（310 aa）	Not recorded	ZN ZINC ION × 6 UTP URIDINE 5'-TRIPHOSPHATE × 6 CTP CYTIDINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions MICRODIALYSIS；pH 5.7；298 K；40 mM sodium citrate, 1 mM 2-mercaptoethanol, 0.2 mM EDTA, 1.0 mM CTP, pH 5.7 (crystals soaked in 5 mM UTP and 5 mM Mg2+), MICRODIALYSIS, temperature 298K	Resolution 1.94 Å R-free 0.236
5AT1 STRUCTURAL CONSEQUENCES OF EFFECTOR BINDING TO THE T STATE OF ASPARTATE CARBAMOYLTRANSFERASE. CRYSTAL STRUCTURES OF THE UNLIGATED AND ATP-, AND CTP-COMPLEXED ENZYMES AT 2.6-ANGSTROMS RESOLUTION Deposited 1990-04-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Not recorded	ZN ZINC ION × 6 CTP CYTIDINE-5'-TRIPHOSPHATE × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.60 Å
6AT1 STRUCTURAL CONSEQUENCES OF EFFECTOR BINDING TO THE T STATE OF ASPARTATE CARBAMOYLTRANSFERASE. CRYSTAL STRUCTURES OF THE UNLIGATED AND ATP-, AND CTP-COMPLEXED ENZYMES AT 2.6-ANGSTROMS RESOLUTION Deposited 1990-04-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Not recorded	ZN ZINC ION × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.60 Å
6KJ7 E. coli ATCase catalytic subunit mutant - G166P Deposited 2019-07-21	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 2–311（310 aa）	Mutation：G166P	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.2M NH4Ac, 0.1 M Tris pH 8.5, 20% PEG3350, and 10% glycerol	Resolution 2.84 Å R-free 0.260
6KJ8 E. coli ATCase holoenzyme mutant - G166P (catalytic chain) Deposited 2019-07-22	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 2–311（310 aa） Chain C 2–311（310 aa） Chain E 2–311（310 aa）	Not recorded	ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.1M HEPES pH 7.0, 30% Jeffamine M-600 pH 7.0, and 10% glycerol	Resolution 3.01 Å R-free 0.247
6KJ9 E. coli ATCase catalytic subunit mutant - G128/130A Deposited 2019-07-22	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 2–311（310 aa） Chain B 2–311（310 aa） Chain E 2–311（310 aa）	Mutation：G128A, G130A Mutation：G128A, G130A Mutation：G128A, G130A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.2M NH4Ac, 0.1M Tris pH 8.5, 20% PEG3350, and 10% glycerol	Resolution 2.50 Å R-free 0.228
6KJ9 E. coli ATCase catalytic subunit mutant - G128/130A Deposited 2019-07-22	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain C 2–311（310 aa） Chain D 2–311（310 aa） Chain F 2–311（310 aa）	Mutation：G128A, G130A Mutation：G128A, G130A Mutation：G128A, G130A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.2M NH4Ac, 0.1M Tris pH 8.5, 20% PEG3350, and 10% glycerol	Resolution 2.50 Å R-free 0.228
6KJA E. coli ATCase holoenzyme mutant - G128/130A (catalytic chain) Deposited 2019-07-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 2–311（310 aa） Chain C 2–311（310 aa） Chain E 2–311（310 aa）	Mutation：G128A, G130A Mutation：G128A, G130A Mutation：G128A, G130A	ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.1 M HEPES pH 7.0, 30% Jeffamine M-600 pH 7.0, and 10% glycerol	Resolution 3.06 Å R-free 0.283
6KJB wild-type apo-form E. coli ATCase holoenzyme with an unusual open conformation of R167 Deposited 2019-07-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 2–311（310 aa）	Not recorded	ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.1M MES pH 6.0 10% Glycerol and 10% PEG 8000	Resolution 2.06 Å R-free 0.223
7AT1 CRYSTAL STRUCTURES OF ASPARTATE CARBAMOYLTRANSFERASE LIGATED WITH PHOSPHONOACETAMIDE, MALONATE, AND CTP OR ATP AT 2.8-ANGSTROMS RESOLUTION AND NEUTRAL P*H Deposited 1989-09-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Not recorded	PCT PHOSPHONOACETAMIDE × 6 ZN ZINC ION × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 3	X-RAY DIFFRACTION X-ray crystallization conditions THE CRYSTALS WERE GROWN IN A SOLUTION OF PHOSPHONACETAMIDE (PAM) AND MALONATE (MAL) AT PH 5.8. THEY WERE THEN SOAKED IN A SOLUTION CONTAINING PAM, MAL, AND ATP AT PH 7.0.	Resolution 2.80 Å
8AT1 CRYSTAL STRUCTURES OF ASPARTATE CARBAMOYLTRANSFERASE LIGATED WITH PHOSPHONOACETAMIDE, MALONATE, AND CTP OR ATP AT 2.8-ANGSTROMS RESOLUTION AND NEUTRAL P*H Deposited 1989-09-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Not recorded	PCT PHOSPHONOACETAMIDE × 6 ZN ZINC ION × 6 CTP CYTIDINE-5'-TRIPHOSPHATE × 6	X-RAY DIFFRACTION X-ray crystallization conditions THE CRYSTALS WERE GROWN IN A SOLUTION OF PHOSPHONACETAMIDE (PAM) AND MALONATE (MAL) AT PH 5.8. THEY WERE THEN SOAKED IN A SOLUTION CONTAINING PAM, MAL, AND CTP AT PH 7.0.	Resolution 2.80 Å
8ATC COMPLEX OF N-PHOSPHONACETYL-L-ASPARTATE WITH ASPARTATE CARBAMOYLTRANSFERASE. X-RAY REFINEMENT, ANALYSIS OF CONFORMATIONAL CHANGES AND CATALYTIC AND ALLOSTERIC MECHANISMS Deposited 1989-08-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa） Chain C 1–310（310 aa）	Not recorded	PAL N-(PHOSPHONACETYL)-L-ASPARTIC ACID × 6 ZN ZINC ION × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
9ATC ATCASE Y165F MUTANT Deposited 1998-06-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–310（310 aa）	Mutation：CHAIN A, Y165F	ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.3；pH 6.3	Resolution 2.40 Å R-free 0.344

59 other PDB entries and 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PYRB_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–311； UniProt 1–311 Author chain B； PDBConstruct 1–311； UniProt 1–311 Author chain C； PDBConstruct 1–311； UniProt 1–311

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	1ekx
Deposition date deposition_date	2000-03-09
Structure title title	THE ISOLATED, UNREGULATED CATALYTIC TRIMER OF ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH BISUBSTRATE ANALOG PALA (N-(PHOSPHONACETYL)-L-ASPARTATE)
Keywords keywords	ATCase catalytic subunit, bisubstrate analog complex, TRANSFERASE; TRANSFERASE
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	31.34 Å
Radius of gyration Rg (electron density) rg_electron	30.51 Å
Forward intensity I(0) i0	168259000.00
Molecular weight molecular_weight	103290.0 kDa
Excluded volume excluded_volume	129240 Å³
Envelope volume envelope_volume	155800 Å³
Hydration-shell volume shell_volume	42129 Å³
Envelope diameter envelope_diameter	96.7 Å
Shell Rg shell_rg	38.26 Å
Envelope Rg envelope_rg	30.44 Å
Shape Rg shape_rg	30.52 Å
Total Rg total_rg	31.08 Å
Total atoms total_atoms	7260
Residues n_residues	925
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	97.9 Å
Rg (real space) rg_real	31.24 Å
Rg uncertainty (real space) rg_real_error	0.56 Å
I(0) (real space) i0_real	1.6830e+08
I(0) uncertainty (real space) i0_real_error	2.5870e+06
Rg (reciprocal space) rg_reciprocal	31.29 Å
I(0) (reciprocal space) i0_reciprocal	168300000.0000
Solution quality estimate total_estimate	0.9055
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	96.0 Å
Skewness Skewness skewness	0.191
Kurtosis Kurtosis kurtosis	-0.645
Angular range angular_range	— – 0.2550 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	110900000.0000
Real-space data points n_real_points	52
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.946; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.932

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	ASPARTATE TRANSCARBAMOYLASE
Molecular weight formula_weight	34468.3 kDa
EC 编号 ec_number	2.1.3.2
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	8084

MANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTSLGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSGNVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMVGDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPQYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEYANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALLALVLNRDLVL

来源 Source

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

Entity 2 Entity 2 non-polymer

Description description	N-(PHOSPHONACETYL)-L-ASPARTIC ACID
Molecular weight formula_weight	255.1 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 3 Entity 3 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	823

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7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d1ekxa1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.78 — ATC-like
Superfamily Superfamily superfamily	c.78.1 — Aspartate/ornithine carbamoyltransferase
Family Family family	c.78.1.1 — Aspartate/ornithine carbamoyltransferase

Domain ID domain_id	d1ekxa2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.78 — ATC-like
Superfamily Superfamily superfamily	c.78.1 — Aspartate/ornithine carbamoyltransferase
Family Family family	c.78.1.1 — Aspartate/ornithine carbamoyltransferase

Domain ID domain_id	d1ekxb1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.78 — ATC-like
Superfamily Superfamily superfamily	c.78.1 — Aspartate/ornithine carbamoyltransferase
Family Family family	c.78.1.1 — Aspartate/ornithine carbamoyltransferase

Domain ID domain_id	d1ekxb2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.78 — ATC-like
Superfamily Superfamily superfamily	c.78.1 — Aspartate/ornithine carbamoyltransferase
Family Family family	c.78.1.1 — Aspartate/ornithine carbamoyltransferase

Domain ID domain_id	d1ekxc1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.78 — ATC-like
Superfamily Superfamily superfamily	c.78.1 — Aspartate/ornithine carbamoyltransferase
Family Family family	c.78.1.1 — Aspartate/ornithine carbamoyltransferase

Domain ID domain_id	d1ekxc2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.78 — ATC-like
Superfamily Superfamily superfamily	c.78.1 — Aspartate/ornithine carbamoyltransferase
Family Family family	c.78.1.1 — Aspartate/ornithine carbamoyltransferase

CATH v4.4 (6 domains)

Domain ID domain_id	1ekxA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1370 — Aspartate/ornithine carbamoyltransferase

Domain ID domain_id	1ekxA02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1370 — Aspartate/ornithine carbamoyltransferase

Domain ID domain_id	1ekxB01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1370 — Aspartate/ornithine carbamoyltransferase

Domain ID domain_id	1ekxB02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1370 — Aspartate/ornithine carbamoyltransferase

Domain ID domain_id	1ekxC01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1370 — Aspartate/ornithine carbamoyltransferase

Domain ID domain_id	1ekxC02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1370 — Aspartate/ornithine carbamoyltransferase

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8. Citations (1)

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Unit-cell length a length_a	58.120 Å
Unit-cell length b length_b	82.130 Å
Unit-cell length c length_c	252.510 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	12

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

Resolution resolution	1.950 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.1710
R_work r_work	0.1710
R_free r_free	0.2140

fit	/app/data/saxs_computation/ek/1ekx/1ekx.fit
pddf	/app/data/pr_computation/ek/1ekx/1ekx.pr.out
profile	/app/data/saxs_computation/ek/1ekx/1ekx.dat