1n3t

Biosynthesis of pteridins. Reaction mechanism of GTP cyclohydrolase I

Method: X-RAY DIFFRACTION D_max: 228.6 Å Quality: REASONABLE

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

GTP cyclohydrolase I

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 × 10 PDB declaration: decameric（10） Consistent with protein copy count	Chain F； UniProt 1–221 Chain G； UniProt 1–221 Chain H； UniProt 1–221 Chain I； UniProt 1–221 Chain J； UniProt 1–221 Chain K； UniProt 1–221 Chain L； UniProt 1–221 Chain M； UniProt 1–221 Chain N； UniProt 1–221 Chain O； UniProt 1–221	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
2	Protein homooligomer Homooligomer Protein × 10 PDB declaration: decameric（10） Consistent with protein copy count	Chain A； UniProt 1–221 Chain B； UniProt 1–221 Chain C； UniProt 1–221 Chain D； UniProt 1–221 Chain E； UniProt 1–221	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

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 1N3T	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1A8R GTP CYCLOHYDROLASE I (H112S MUTANT) IN COMPLEX WITH GTP Deposited 1998-03-27	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	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	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	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	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	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	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	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	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	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	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	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	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	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	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: eicosameric	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	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	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	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	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	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	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	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	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	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	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	Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	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	Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	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	Different mutation/modification Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	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

6 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	GCH1_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–221； UniProt 1–221 Author chain B； PDBConstruct 1–221； UniProt 1–221 Author chain C； PDBConstruct 1–221； UniProt 1–221 Author chain D； PDBConstruct 1–221； UniProt 1–221 Author chain E； PDBConstruct 1–221； UniProt 1–221 Author chain F； PDBConstruct 1–221； UniProt 1–221 Author chain G； PDBConstruct 1–221； UniProt 1–221 Author chain H； PDBConstruct 1–221； UniProt 1–221 Author chain I； PDBConstruct 1–221； UniProt 1–221 Author chain J； PDBConstruct 1–221； UniProt 1–221 Author chain K； PDBConstruct 1–221； UniProt 1–221 Author chain L； PDBConstruct 1–221； UniProt 1–221 Author chain M； PDBConstruct 1–221； UniProt 1–221 Author chain N； PDBConstruct 1–221； UniProt 1–221 Author chain O； PDBConstruct 1–221； UniProt 1–221

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	1n3t
Deposition date deposition_date	2002-10-29
Structure title title	Biosynthesis of pteridins. Reaction mechanism of GTP cyclohydrolase I
Keywords keywords	Biosynthesis, folic acid, GTP cyclohydrolase I, tetrahydropterin, pteridines, HYDROLASE; HYDROLASE
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	90.59 Å
Radius of gyration Rg (electron density) rg_electron	92.86 Å
Forward intensity I(0) i0	2074210000.00
Molecular weight molecular_weight	378080.0 kDa
Excluded volume excluded_volume	470200 Å³
Envelope volume envelope_volume	817520 Å³
Hydration-shell volume shell_volume	75605 Å³
Envelope diameter envelope_diameter	291.2 Å
Shell Rg shell_rg	82.05 Å
Envelope Rg envelope_rg	91.77 Å
Shape Rg shape_rg	92.85 Å
Total Rg total_rg	92.77 Å
Total atoms total_atoms	26475
Residues n_residues	3315
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	228.6 Å
Rg (real space) rg_real	87.13 Å
Rg uncertainty (real space) rg_real_error	1.48 Å
I(0) (real space) i0_real	2.0100e+09
I(0) uncertainty (real space) i0_real_error	4.7380e+07
Rg (reciprocal space) rg_reciprocal	80.80 Å
I(0) (reciprocal space) i0_reciprocal	2014000000.0000
Solution quality estimate total_estimate	0.6469
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	53.8 Å
Skewness Skewness skewness	0.368
Kurtosis Kurtosis kurtosis	-1.465
Angular range angular_range	— – 0.0850 Å⁻¹
Current regularization parameter α current_alpha	0.0335
Highest regularization parameter α highest_alpha	56810000.0000
Real-space data points n_real_points	18
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.001; Oscil: 0.007; Stabil: 0.764; Sysdev: 1.000; Positv: 1.000; Valcen: 0.209; Smooth: 0.900

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 45 domains

SCOP 2.08 (15 domains)

Domain ID domain_id	d1n3ta_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.96 — T-fold
Superfamily Superfamily superfamily	d.96.1 — Tetrahydrobiopterin biosynthesis enzymes-like
Family Family family	d.96.1.1 — GTP cyclohydrolase I

Domain ID domain_id	d1n3tb_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.96 — T-fold
Superfamily Superfamily superfamily	d.96.1 — Tetrahydrobiopterin biosynthesis enzymes-like
Family Family family	d.96.1.1 — GTP cyclohydrolase I

Domain ID domain_id	d1n3tc_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.96 — T-fold
Superfamily Superfamily superfamily	d.96.1 — Tetrahydrobiopterin biosynthesis enzymes-like
Family Family family	d.96.1.1 — GTP cyclohydrolase I

Domain ID domain_id	d1n3td_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.96 — T-fold
Superfamily Superfamily superfamily	d.96.1 — Tetrahydrobiopterin biosynthesis enzymes-like
Family Family family	d.96.1.1 — GTP cyclohydrolase I

Domain ID domain_id	d1n3te_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.96 — T-fold
Superfamily Superfamily superfamily	d.96.1 — Tetrahydrobiopterin biosynthesis enzymes-like
Family Family family	d.96.1.1 — GTP cyclohydrolase I

Domain ID domain_id	d1n3tf_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.96 — T-fold
Superfamily Superfamily superfamily	d.96.1 — Tetrahydrobiopterin biosynthesis enzymes-like
Family Family family	d.96.1.1 — GTP cyclohydrolase I

Domain ID domain_id	d1n3tg_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.96 — T-fold
Superfamily Superfamily superfamily	d.96.1 — Tetrahydrobiopterin biosynthesis enzymes-like
Family Family family	d.96.1.1 — GTP cyclohydrolase I

Domain ID domain_id	d1n3th_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.96 — T-fold
Superfamily Superfamily superfamily	d.96.1 — Tetrahydrobiopterin biosynthesis enzymes-like
Family Family family	d.96.1.1 — GTP cyclohydrolase I

Domain ID domain_id	d1n3ti_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.96 — T-fold
Superfamily Superfamily superfamily	d.96.1 — Tetrahydrobiopterin biosynthesis enzymes-like
Family Family family	d.96.1.1 — GTP cyclohydrolase I

Domain ID domain_id	d1n3tj_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.96 — T-fold
Superfamily Superfamily superfamily	d.96.1 — Tetrahydrobiopterin biosynthesis enzymes-like
Family Family family	d.96.1.1 — GTP cyclohydrolase I

Domain ID domain_id	d1n3tk_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.96 — T-fold
Superfamily Superfamily superfamily	d.96.1 — Tetrahydrobiopterin biosynthesis enzymes-like
Family Family family	d.96.1.1 — GTP cyclohydrolase I

Domain ID domain_id	d1n3tl_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.96 — T-fold
Superfamily Superfamily superfamily	d.96.1 — Tetrahydrobiopterin biosynthesis enzymes-like
Family Family family	d.96.1.1 — GTP cyclohydrolase I

Domain ID domain_id	d1n3tm_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.96 — T-fold
Superfamily Superfamily superfamily	d.96.1 — Tetrahydrobiopterin biosynthesis enzymes-like
Family Family family	d.96.1.1 — GTP cyclohydrolase I

Domain ID domain_id	d1n3tn_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.96 — T-fold
Superfamily Superfamily superfamily	d.96.1 — Tetrahydrobiopterin biosynthesis enzymes-like
Family Family family	d.96.1.1 — GTP cyclohydrolase I

Domain ID domain_id	d1n3to_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.96 — T-fold
Superfamily Superfamily superfamily	d.96.1 — Tetrahydrobiopterin biosynthesis enzymes-like
Family Family family	d.96.1.1 — GTP cyclohydrolase I

CATH v4.4 (30 domains)

Domain ID domain_id	1n3tA01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	286 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, N-terminal domain

Domain ID domain_id	1n3tA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1130 — GTP Cyclohydrolase I, domain 2
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain

Domain ID domain_id	1n3tB01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	286 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, N-terminal domain

Domain ID domain_id	1n3tB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1130 — GTP Cyclohydrolase I, domain 2
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain

Domain ID domain_id	1n3tC01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	286 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, N-terminal domain

Domain ID domain_id	1n3tC02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1130 — GTP Cyclohydrolase I, domain 2
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain

Domain ID domain_id	1n3tD01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	286 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, N-terminal domain

Domain ID domain_id	1n3tD02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1130 — GTP Cyclohydrolase I, domain 2
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain

Domain ID domain_id	1n3tE01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	286 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, N-terminal domain

Domain ID domain_id	1n3tE02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1130 — GTP Cyclohydrolase I, domain 2
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain

Domain ID domain_id	1n3tF01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	286 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, N-terminal domain

Domain ID domain_id	1n3tF02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1130 — GTP Cyclohydrolase I, domain 2
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain

Domain ID domain_id	1n3tG01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	286 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, N-terminal domain

Domain ID domain_id	1n3tG02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1130 — GTP Cyclohydrolase I, domain 2
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain

Domain ID domain_id	1n3tH01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	286 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, N-terminal domain

Domain ID domain_id	1n3tH02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1130 — GTP Cyclohydrolase I, domain 2
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain

Domain ID domain_id	1n3tI01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	286 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, N-terminal domain

Domain ID domain_id	1n3tI02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1130 — GTP Cyclohydrolase I, domain 2
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain

Domain ID domain_id	1n3tJ01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	286 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, N-terminal domain

Domain ID domain_id	1n3tJ02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1130 — GTP Cyclohydrolase I, domain 2
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain

Domain ID domain_id	1n3tK01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	286 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, N-terminal domain

Domain ID domain_id	1n3tK02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1130 — GTP Cyclohydrolase I, domain 2
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain

Domain ID domain_id	1n3tL01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	286 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, N-terminal domain

Domain ID domain_id	1n3tL02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1130 — GTP Cyclohydrolase I, domain 2
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain

Domain ID domain_id	1n3tM01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	286 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, N-terminal domain

Domain ID domain_id	1n3tM02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1130 — GTP Cyclohydrolase I, domain 2
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain

Domain ID domain_id	1n3tN01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	286 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, N-terminal domain

Domain ID domain_id	1n3tN02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1130 — GTP Cyclohydrolase I, domain 2
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain

Domain ID domain_id	1n3tO01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	286 — GTP Cyclohydrolase I; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, N-terminal domain

Domain ID domain_id	1n3tO02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1130 — GTP Cyclohydrolase I, domain 2
Homologous superfamily homologous superfamily	10 — GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain

▶

8. Citations (1)

▶

Unit-cell length a length_a	223.140 Å
Unit-cell length b length_b	317.810 Å
Unit-cell length c length_c	132.150 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	120

Space group space_group	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	3.200 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.1850
R_work r_work	0.1850
R_free r_free	0.2280

Description description	GTP cyclohydrolase I
Molecular weight formula_weight	24717.4 kDa
EC 编号 ec_number	3.5.4.16
Mutation mutation	C181S
Source method src_method	man
Copy count entity_count	15

Polymer type type	polypeptide(L)
Chain IDs strand_id	F,G,H,I,J,K,L,M,N,O,A,B,C,D,E
Atom count atom_count	26475

Biosynthesis of pteridins. Reaction mechanism of GTP cyclohydrolase I

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

GTP cyclohydrolase I

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 non-polymer

7. Fold Classification (SCOP + CATH) 45 domains

SCOP 2.08 (15 domains)

CATH v4.4 (30 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

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

Description description	GUANOSINE-5'-TRIPHOSPHATE
Molecular weight formula_weight	523.2 kDa
Source method src_method	syn
Copy count entity_count	15

fit	/app/data/saxs_computation/n3/1n3t/1n3t.fit
pddf	/app/data/pr_computation/n3/1n3t/1n3t.pr.out
profile	/app/data/saxs_computation/n3/1n3t/1n3t.dat