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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：P0A6T5 New Search
7PDB entries
19Biological assembly
150chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental conditions Different structure-quality metrics

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
1A8R GTP CYCLOHYDROLASE I (H112S MUTANT) IN COMPLEX WITH GTP Deposited 1998-03-27 Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric（10） Consistent with protein count
Chain A 1–221（221 aa）
Chain B 1–221（221 aa）
Chain C 1–221（221 aa）
Chain D 1–221（221 aa）
Chain E 1–221（221 aa）
Mutation：H112S Mutation：H112S Mutation：H112S Mutation：H112S Mutation：H112S GTP GUANOSINE-5'-TRIPHOSPHATE × 10 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；pH 7.0
Resolution 2.10 Å R-free 0.246
1A8R GTP CYCLOHYDROLASE I (H112S MUTANT) IN COMPLEX WITH GTP Deposited 1998-03-27 Assembly 2 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric（10） Consistent with protein count
Chain F 1–221（221 aa）
Chain G 1–221（221 aa）
Chain H 1–221（221 aa）
Chain I 1–221（221 aa）
Chain J 1–221（221 aa）
Chain K 1–221（221 aa）
Chain L 1–221（221 aa）
Chain M 1–221（221 aa）
Chain N 1–221（221 aa）
Chain O 1–221（221 aa）
Mutation：H112S Mutation：H112S Mutation：H112S Mutation：H112S Mutation：H112S Mutation：H112S Mutation：H112S Mutation：H112S Mutation：H112S Mutation：H112S GTP GUANOSINE-5'-TRIPHOSPHATE × 10 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；pH 7.0
Resolution 2.10 Å R-free 0.246
1A9C GTP CYCLOHYDROLASE I (C110S MUTANT) IN COMPLEX WITH GTP Deposited 1998-04-04 Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric（10） Consistent with protein count
Chain A 1–221（221 aa）
Chain B 1–221（221 aa）
Chain C 1–221（221 aa）
Chain D 1–221（221 aa）
Chain E 1–221（221 aa）
Mutation：C110S Mutation：C110S Mutation：C110S Mutation：C110S Mutation：C110S GTP GUANOSINE-5'-TRIPHOSPHATE × 10 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；pH 7.0
Resolution 2.90 Å R-free 0.288
1A9C GTP CYCLOHYDROLASE I (C110S MUTANT) IN COMPLEX WITH GTP Deposited 1998-04-04 Assembly 2 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric（10） Consistent with protein count
Chain F 1–221（221 aa）
Chain G 1–221（221 aa）
Chain H 1–221（221 aa）
Chain I 1–221（221 aa）
Chain J 1–221（221 aa）
Chain K 1–221（221 aa）
Chain L 1–221（221 aa）
Chain M 1–221（221 aa）
Chain N 1–221（221 aa）
Chain O 1–221（221 aa）
Mutation：C110S Mutation：C110S Mutation：C110S Mutation：C110S Mutation：C110S Mutation：C110S Mutation：C110S Mutation：C110S Mutation：C110S Mutation：C110S GTP GUANOSINE-5'-TRIPHOSPHATE × 10 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；pH 7.0
Resolution 2.90 Å R-free 0.288
1FBX CRYSTAL STRUCTURE OF ZINC-CONTAINING E.COLI GTP CYCLOHYDROLASE I Deposited 2000-07-17 Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric（10） Consistent with protein count
Chain A 2–222（221 aa）
Chain B 2–222（221 aa）
Chain C 2–222（221 aa）
Chain D 2–222（221 aa）
Chain E 2–222（221 aa）
Not recorded ZN ZINC ION × 10 CL CHLORIDE ION × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；298 K；PEG 6000, KCL, MOPS, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 298.0K
Resolution 2.80 Å R-free 0.251
1FBX CRYSTAL STRUCTURE OF ZINC-CONTAINING E.COLI GTP CYCLOHYDROLASE I Deposited 2000-07-17 Assembly 2 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric（10） Consistent with protein count
Chain F 2–222（221 aa）
Chain G 2–222（221 aa）
Chain H 2–222（221 aa）
Chain I 2–222（221 aa）
Chain J 2–222（221 aa）
Chain K 2–222（221 aa）
Chain L 2–222（221 aa）
Chain M 2–222（221 aa）
Chain N 2–222（221 aa）
Chain O 2–222（221 aa）
Not recorded ZN ZINC ION × 10 CL CHLORIDE ION × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；298 K；PEG 6000, KCL, MOPS, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 298.0K
Resolution 2.80 Å R-free 0.251
1GTP GTP CYCLOHYDROLASE I Deposited 1995-09-16 Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric（10） Consistent with protein count
Chain A 1–221（221 aa）
Chain B 1–221（221 aa）
Chain C 1–221（221 aa）
Chain D 1–221（221 aa）
Chain E 1–221（221 aa）
Chain F 1–221（221 aa）
Chain G 1–221（221 aa）
Chain H 1–221（221 aa）
Chain I 1–221（221 aa）
Chain J 1–221（221 aa）
Not recorded SO4 SULFATE ION × 10 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；pH 7.0
Resolution 3.00 Å
1GTP GTP CYCLOHYDROLASE I Deposited 1995-09-16 Assembly 2 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric（10） Consistent with protein count
Chain K 1–221（221 aa）
Chain L 1–221（221 aa）
Chain M 1–221（221 aa）
Chain N 1–221（221 aa）
Chain O 1–221（221 aa）
Chain P 1–221（221 aa）
Chain Q 1–221（221 aa）
Chain R 1–221（221 aa）
Chain S 1–221（221 aa）
Chain T 1–221（221 aa）
Not recorded SO4 SULFATE ION × 10 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；pH 7.0
Resolution 3.00 Å
1GTP GTP CYCLOHYDROLASE I Deposited 1995-09-16 Assembly 3 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: eicosameric（20） Consistent with protein count
Chain A 1–221（221 aa）
Chain B 1–221（221 aa）
Chain C 1–221（221 aa）
Chain D 1–221（221 aa）
Chain E 1–221（221 aa）
Chain F 1–221（221 aa）
Chain G 1–221（221 aa）
Chain H 1–221（221 aa）
Chain I 1–221（221 aa）
Chain J 1–221（221 aa）
Chain K 1–221（221 aa）
Chain L 1–221（221 aa）
Chain M 1–221（221 aa）
Chain N 1–221（221 aa）
Chain O 1–221（221 aa）
Chain P 1–221（221 aa）
Chain Q 1–221（221 aa）
Chain R 1–221（221 aa）
Chain S 1–221（221 aa）
Chain T 1–221（221 aa）
Not recorded SO4 SULFATE ION × 20 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；pH 7.0
Resolution 3.00 Å
1N3R Biosynthesis of pteridins. Reaction mechanism of GTP cyclohydrolase I Deposited 2002-10-29 Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain A 1–221（221 aa）
Chain B 1–221（221 aa）
Chain C 1–221（221 aa）
Chain D 1–221（221 aa）
Chain E 1–221（221 aa）
Mutation：H112S Mutation：H112S Mutation：H112S Mutation：H112S Mutation：H112S GTP GUANOSINE-5'-TRIPHOSPHATE × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.2；293 K；Peg 6000, pH 8.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.80 Å R-free 0.272
1N3R Biosynthesis of pteridins. Reaction mechanism of GTP cyclohydrolase I Deposited 2002-10-29 Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain F 1–221（221 aa）
Chain G 1–221（221 aa）
Chain H 1–221（221 aa）
Chain I 1–221（221 aa）
Chain J 1–221（221 aa）
Mutation：H112S Mutation：H112S Mutation：H112S Mutation：H112S Mutation：H112S GTP GUANOSINE-5'-TRIPHOSPHATE × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.2；293 K；Peg 6000, pH 8.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.80 Å R-free 0.272
1N3R Biosynthesis of pteridins. Reaction mechanism of GTP cyclohydrolase I Deposited 2002-10-29 Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain K 1–221（221 aa）
Chain L 1–221（221 aa）
Chain M 1–221（221 aa）
Chain N 1–221（221 aa）
Chain O 1–221（221 aa）
Mutation：H112S Mutation：H112S Mutation：H112S Mutation：H112S Mutation：H112S GTP GUANOSINE-5'-TRIPHOSPHATE × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.2；293 K；Peg 6000, pH 8.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.80 Å R-free 0.272
1N3R Biosynthesis of pteridins. Reaction mechanism of GTP cyclohydrolase I Deposited 2002-10-29 Assembly 4 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric（10） Consistent with protein count
Chain A 1–221（221 aa）
Chain B 1–221（221 aa）
Chain C 1–221（221 aa）
Chain D 1–221（221 aa）
Chain E 1–221（221 aa）
Chain F 1–221（221 aa）
Chain G 1–221（221 aa）
Chain H 1–221（221 aa）
Chain I 1–221（221 aa）
Chain J 1–221（221 aa）
Mutation：H112S Mutation：H112S Mutation：H112S Mutation：H112S Mutation：H112S Mutation：H112S Mutation：H112S Mutation：H112S Mutation：H112S Mutation：H112S GTP GUANOSINE-5'-TRIPHOSPHATE × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.2；293 K；Peg 6000, pH 8.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.80 Å R-free 0.272
1N3R Biosynthesis of pteridins. Reaction mechanism of GTP cyclohydrolase I Deposited 2002-10-29 Assembly 5 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric（10） Consistent with protein count
Chain K 1–221（221 aa）
Chain L 1–221（221 aa）
Chain M 1–221（221 aa）
Chain N 1–221（221 aa）
Chain O 1–221（221 aa）
Mutation：H112S Mutation：H112S Mutation：H112S Mutation：H112S Mutation：H112S GTP GUANOSINE-5'-TRIPHOSPHATE × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.2；293 K；Peg 6000, pH 8.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.80 Å R-free 0.272
1N3S Biosynthesis of pteridins. Reaction mechanism of GTP cyclohydrolase I Deposited 2002-10-29 Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain A 1–221（221 aa）
Chain B 1–221（221 aa）
Chain C 1–221（221 aa）
Chain D 1–221（221 aa）
Chain E 1–221（221 aa）
Mutation：H113S Mutation：H113S Mutation：H113S Mutation：H113S Mutation：H113S GTP GUANOSINE-5'-TRIPHOSPHATE × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.2；293 K；Peg6000, pH 8.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.55 Å R-free 0.293
1N3S Biosynthesis of pteridins. Reaction mechanism of GTP cyclohydrolase I Deposited 2002-10-29 Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain F 1–221（221 aa）
Chain G 1–221（221 aa）
Chain H 1–221（221 aa）
Chain I 1–221（221 aa）
Chain J 1–221（221 aa）
Mutation：H113S Mutation：H113S Mutation：H113S Mutation：H113S Mutation：H113S GTP GUANOSINE-5'-TRIPHOSPHATE × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.2；293 K；Peg6000, pH 8.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.55 Å R-free 0.293
1N3S Biosynthesis of pteridins. Reaction mechanism of GTP cyclohydrolase I Deposited 2002-10-29 Assembly 3 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric（10） Consistent with protein count
Chain A 1–221（221 aa）
Chain B 1–221（221 aa）
Chain C 1–221（221 aa）
Chain D 1–221（221 aa）
Chain E 1–221（221 aa）
Chain F 1–221（221 aa）
Chain G 1–221（221 aa）
Chain H 1–221（221 aa）
Chain I 1–221（221 aa）
Chain J 1–221（221 aa）
Mutation：H113S Mutation：H113S Mutation：H113S Mutation：H113S Mutation：H113S Mutation：H113S Mutation：H113S Mutation：H113S Mutation：H113S Mutation：H113S GTP GUANOSINE-5'-TRIPHOSPHATE × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.2；293 K；Peg6000, pH 8.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.55 Å R-free 0.293
1N3T Biosynthesis of pteridins. Reaction mechanism of GTP cyclohydrolase I Deposited 2002-10-29 Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric（10） Consistent with protein count
Chain F 1–221（221 aa）
Chain G 1–221（221 aa）
Chain H 1–221（221 aa）
Chain I 1–221（221 aa）
Chain J 1–221（221 aa）
Chain K 1–221（221 aa）
Chain L 1–221（221 aa）
Chain M 1–221（221 aa）
Chain N 1–221（221 aa）
Chain O 1–221（221 aa）
Mutation：C181S Mutation：C181S Mutation：C181S Mutation：C181S Mutation：C181S Mutation：C181S Mutation：C181S Mutation：C181S Mutation：C181S Mutation：C181S GTP GUANOSINE-5'-TRIPHOSPHATE × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.2；293 K；Peg6000, pH 8.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 3.20 Å R-free 0.228
1N3T Biosynthesis of pteridins. Reaction mechanism of GTP cyclohydrolase I Deposited 2002-10-29 Assembly 2 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric（10） Consistent with protein count
Chain A 1–221（221 aa）
Chain B 1–221（221 aa）
Chain C 1–221（221 aa）
Chain D 1–221（221 aa）
Chain E 1–221（221 aa）
Mutation：C181S Mutation：C181S Mutation：C181S Mutation：C181S Mutation：C181S GTP GUANOSINE-5'-TRIPHOSPHATE × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.2；293 K；Peg6000, pH 8.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 3.20 Å R-free 0.228

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.