Aspartate carbamoyltransferase catalytic chain
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 × 12 PDB declaration: dodecameric（12） Consistent with protein copy count | Chain A； UniProt 1–310 Chain C； UniProt 1–310 | Mutation：E50A | Aspartate carbamoyltransferase regulatory chain × 6 （P0A7F3） 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 |
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 1TUG | 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 mutation/modification 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 mutation/modification 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 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 |
| 1EKX THE ISOLATED, UNREGULATED CATALYTIC TRIMER OF ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH BISUBSTRATE ANALOG PALA (N-(PHOSPHONACETYL)-L-ASPARTATE) Deposited 2000-03-09 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric |
Chain A
1–311（311 aa）
Fragment：CATALYTIC SUBUNIT
Chain B
1–311（311 aa）
Fragment：CATALYTIC SUBUNIT
Chain C
1–311（311 aa）
Fragment：CATALYTIC SUBUNIT
|
Not recorded | 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 |
| 1EZZ CRYSTAL STRUCTURE OF E. COLI ASPARTATE TRANSCARBAMOYLASE P268A MUTANT IN THE T-STATE Deposited 2000-05-12 | Different mutation/modification 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 mutation/modification 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 mutation/modification 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 mutation/modification 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 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 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 mutation/modification 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 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 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 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 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 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 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 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 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 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 mutation/modification 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 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 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 |
| 1XJW The Structure of E. coli Aspartate Transcarbamoylase Q137A Mutant in The R-State Deposited 2004-09-25 | Different mutation/modification 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 mutation/modification 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 mutation/modification 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 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 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 mutation/modification 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 mutation/modification 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 mutation/modification 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 mutation/modification 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 mutation/modification 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 mutation/modification 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 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 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 mutation/modification 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 mutation/modification Different oligomeric state 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 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 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 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 mutation/modification 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 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 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 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 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 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 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 mutation/modification 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 mutation/modification 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 oligomeric state 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 mutation/modification 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 oligomeric state 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 oligomeric state 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 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 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 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 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 mutation/modification 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 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 1–310； UniProt 1–310 Author chain C； PDBConstruct 1–310； UniProt 1–310 |
