Current Protein Identity:P08179
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Difference tags compare only the current result set; every original PDB and assembly record remains separate.
Related-Structure Differences
Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.
| PDB Entry | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Experimental Method | Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 1C2T NEW INSIGHTS INTO INHIBITOR DESIGN FROM THE CRYSTAL STRUCTURE AND NMR STUDIES OF E. COLI GAR TRANSFORMYLASE IN COMPLEX WITH BETA-GAR AND 10-FORMYL-5,8,10-TRIDEAZAFOLIC ACID. Deposited 1999-07-26 | Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain A
1–212(212 aa)
Chain B
1–212(212 aa)
|
Not recorded | NHS 10-FORMYL-5,8,10-TRIDEAZAFOLIC ACID × 2 GAR GLYCINAMIDE RIBONUCLEOTIDE × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;pH 7.2;295 K;PEG 3350, IMIDAZOLE MALATE, CALCIUM CHLORIDE, MPD, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 22.0K, temperature 295K
|
Resolution 2.10 Å R-free 0.265 |
| 1C3E NEW INSIGHTS INTO INHIBITOR DESIGN FROM THE CRYSTAL STRUCTURE AND NMR STUDIES OF E. COLI GAR TRANSFORMYLATE IN COMPLEX WITH BETA-GAR AND 10-FORMYL-5,8,10-TRIDEAZAFOLIC ACID. Deposited 1999-07-27 | Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain not uniquely mapped
Reference range not declared
Chain A
1–209(209 aa)
|
Not recorded | NHR 2-{4-[2-(2-AMINO-4-HYDROXY-QUINAZOLIN-6-YL)-1-CARBOXY-ETHYL]-BENZOYLAMINO}-PENTANEDIOIC ACID × 2 GAR GLYCINAMIDE RIBONUCLEOTIDE × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;pH 7.2;295 K;PEG 3350, Imidazole malate, calcium chloride, MPD, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 22.0K
|
Resolution 2.10 Å R-free 0.263 |
| 1CDD STRUCTURES OF APO AND COMPLEXED ESCHERICHIA COLI GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE Deposited 1992-05-15 | Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain A
1–212(212 aa)
Chain B
1–212(212 aa)
|
Not recorded | PO4 PHOSPHATE ION × 2 | X-RAY DIFFRACTION | mmCIF provides none of the parsed conditions | Resolution 2.80 Å |
| 1CDD STRUCTURES OF APO AND COMPLEXED ESCHERICHIA COLI GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE Deposited 1992-05-15 | Assembly 2 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain A
1–212(212 aa)
Chain B
1–212(212 aa)
|
Not recorded | PO4 PHOSPHATE ION × 2 | X-RAY DIFFRACTION | mmCIF provides none of the parsed conditions | Resolution 2.80 Å |
| 1CDE STRUCTURES OF APO AND COMPLEXED ESCHERICHIA COLI GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE Deposited 1992-05-15 | Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain A
1–212(212 aa)
|
Not recorded | GAR GLYCINAMIDE RIBONUCLEOTIDE × 1 DZF 5-DEAZAFOLIC ACID × 1 | X-RAY DIFFRACTION | mmCIF provides none of the parsed conditions | Resolution 2.50 Å |
| 1CDE STRUCTURES OF APO AND COMPLEXED ESCHERICHIA COLI GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE Deposited 1992-05-15 | Assembly 2 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain B
1–212(212 aa)
|
Not recorded | GAR GLYCINAMIDE RIBONUCLEOTIDE × 1 DZF 5-DEAZAFOLIC ACID × 1 | X-RAY DIFFRACTION | mmCIF provides none of the parsed conditions | Resolution 2.50 Å |
| 1CDE STRUCTURES OF APO AND COMPLEXED ESCHERICHIA COLI GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE Deposited 1992-05-15 | Assembly 3 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain C
1–212(212 aa)
|
Not recorded | GAR GLYCINAMIDE RIBONUCLEOTIDE × 1 DZF 5-DEAZAFOLIC ACID × 1 | X-RAY DIFFRACTION | mmCIF provides none of the parsed conditions | Resolution 2.50 Å |
| 1CDE STRUCTURES OF APO AND COMPLEXED ESCHERICHIA COLI GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE Deposited 1992-05-15 | Assembly 4 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain D
1–212(212 aa)
|
Not recorded | GAR GLYCINAMIDE RIBONUCLEOTIDE × 1 DZF 5-DEAZAFOLIC ACID × 1 | X-RAY DIFFRACTION | mmCIF provides none of the parsed conditions | Resolution 2.50 Å |
| 1GAR TOWARDS STRUCTURE-BASED DRUG DESIGN: CRYSTAL STRUCTURE OF A MULTISUBSTRATE ADDUCT COMPLEX OF GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE AT 1.96 ANGSTROMS RESOLUTION Deposited 1994-12-08 | Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain A
1–212(212 aa)
Chain B
1–212(212 aa)
|
Not recorded | U89 N-[4-[[3-(2,4-DIAMINO-1,6-DIHYDRO-6-OXO-4-PYRIMIDINYL)-PROPYL]-[2-((2-OXO-2-((4-PHOSPHORIBOXY)-BUTYL)-AMINO)-ETHYL)-THIO-ACETYL]-AMINO]BENZOYL]-1-GLUTAMIC ACID × 2 | X-RAY DIFFRACTION | mmCIF provides none of the parsed conditions | Resolution 1.96 Å R-free 0.290 |
| 1GRC CRYSTAL STRUCTURE OF GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE FROM ESCHERICHIA COLI AT 3.0 ANGSTROMS RESOLUTION: A TARGET ENZYME FOR CHEMOTHERAPY Deposited 1992-07-21 | Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain A
1–212(212 aa)
Chain B
1–212(212 aa)
|
Not recorded | PO4 PHOSPHATE ION × 2 | X-RAY DIFFRACTION | mmCIF provides none of the parsed conditions | Resolution 3.00 Å |
| 1JKX Unexpected formation of an epoxide-derived multisubstrate adduct inhibitor on the active site of GAR transformylase Deposited 2001-07-13 | Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain A
1–212(212 aa)
Fragment:TRANSFERASE
Chain B
1–212(212 aa)
Fragment:TRANSFERASE
|
Not recorded | 138 N-[5'-O-PHOSPHONO-RIBOFURANOSYL]-2-[2-HYDROXY-2-[4-[GLUTAMIC ACID]-N-CARBONYLPHENYL]-3-[2-AMINO-4-HYDROXY-QUINAZOLIN-6-YL]-PROPANYLAMINO]-ACETAMIDE × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;pH 7.4;295 K;PEG 3350, CaCl2, MPD, imidazole malate, PH 7.4, VAPOR DIFFUSION, SITTING DROP at 295K
|
Resolution 1.60 Å R-free 0.243 |
| 1JKX Unexpected formation of an epoxide-derived multisubstrate adduct inhibitor on the active site of GAR transformylase Deposited 2001-07-13 | Assembly 2 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain C
1–212(212 aa)
Fragment:TRANSFERASE
Chain D
1–212(212 aa)
Fragment:TRANSFERASE
|
Not recorded | 138 N-[5'-O-PHOSPHONO-RIBOFURANOSYL]-2-[2-HYDROXY-2-[4-[GLUTAMIC ACID]-N-CARBONYLPHENYL]-3-[2-AMINO-4-HYDROXY-QUINAZOLIN-6-YL]-PROPANYLAMINO]-ACETAMIDE × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;pH 7.4;295 K;PEG 3350, CaCl2, MPD, imidazole malate, PH 7.4, VAPOR DIFFUSION, SITTING DROP at 295K
|
Resolution 1.60 Å R-free 0.243 |
| 2GAR A PH-DEPENDENT STABLIZATION OF AN ACTIVE SITE LOOP OBSERVED FROM LOW AND HIGH PH CRYSTAL STRUCTURES OF MUTANT MONOMERIC GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE Deposited 1998-05-13 | Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain A
1–212(212 aa)
|
Mutation:E70A | PO4 PHOSPHATE ION × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 3.5;CRYSTAL GREW FROM A SOLUTION OF 2%(V/V) 15% (W/V) PEG 1500, PH 3.5
|
Resolution 1.80 Å R-free 0.251 |
| 3GAR A PH-DEPENDENT STABLIZATION OF AN ACTIVE SITE LOOP OBSERVED FROM LOW AND HIGH PH CRYSTAL STRUCTURES OF MUTANT MONOMERIC GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE Deposited 1998-05-13 | Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain A
1–212(212 aa)
|
Mutation:E70A | PO4 PHOSPHATE ION × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 7.5;CRYSTAL GREW FROM A SOLUTION OF 2%(V/V) PEG 400. 2.0M AMMONIUM SULFATE, 0.1M HEPES, PH 7.5
|
Resolution 1.90 Å R-free 0.274 |