1n3s

Biosynthesis of pteridins. Reaction mechanism of GTP cyclohydrolase I

Method: X-RAY DIFFRACTION D_max: 210.1 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 × 5 PDB declaration: pentameric（5） 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：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
2	Protein homooligomer Homooligomer Protein × 5 PDB declaration: pentameric（5） 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	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
3	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 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	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

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 1N3S	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 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 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 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
1N3T Biosynthesis of pteridins. Reaction mechanism of GTP cyclohydrolase I Deposited 2002-10-29	Different mutation/modification Different structure-quality metrics	Assembly 1 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：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	Different mutation/modification Different structure-quality metrics	Assembly 2 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：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

6 other PDB entries and 16 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

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	1n3s
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	88.46 Å
Radius of gyration Rg (electron density) rg_electron	89.56 Å
Forward intensity I(0) i0	917826000.00
Molecular weight molecular_weight	251720.0 kDa
Excluded volume excluded_volume	313010 Å³
Envelope volume envelope_volume	642340 Å³
Hydration-shell volume shell_volume	59297 Å³
Envelope diameter envelope_diameter	264.3 Å
Shell Rg shell_rg	95.32 Å
Envelope Rg envelope_rg	82.47 Å
Shape Rg shape_rg	89.55 Å
Total Rg total_rg	89.62 Å
Total atoms total_atoms	17610
Residues n_residues	2210
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	210.1 Å
Rg (real space) rg_real	85.35 Å
Rg uncertainty (real space) rg_real_error	1.17 Å
I(0) (real space) i0_real	8.9110e+08
I(0) uncertainty (real space) i0_real_error	1.7650e+07
Rg (reciprocal space) rg_reciprocal	82.45 Å
I(0) (reciprocal space) i0_reciprocal	901200000.0000
Solution quality estimate total_estimate	0.6010
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	46.7 Å
Skewness Skewness skewness	0.127
Kurtosis Kurtosis kurtosis	-1.571
Angular range angular_range	— – 0.0900 Å⁻¹
Current regularization parameter α current_alpha	0.0271
Highest regularization parameter α highest_alpha	17450000.0000
Real-space data points n_real_points	19
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.007; Stabil: 0.839; Sysdev: 1.000; Positv: 1.000; Valcen: 0.009; Smooth: 0.379

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	GTP cyclohydrolase I
Molecular weight formula_weight	24682.4 kDa
EC 编号 ec_number	3.5.4.16
Mutation mutation	H113S
Source method src_method	man
Copy count entity_count	10

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J
Atom count atom_count	17795

PSLSKEAALVHEALVARGLETPLRPPVHEMDNETRKSLIAGHMTEIMQLLNLDLADDSLMETPHRIAKMYVDEIFSGLDYANFPKITLIENKMKVDEMVTVRDITLTSTCEHSFVTIDGKATVAYIPKDSVIGLSKINRIVQFFAQRPQVQERLTQQILIALQTLLGTNNVAVSIDAVHYCVKARGIRDATSATTTTSLGGLFKSSQNTRHEFLRAVRHHN

来源 Source

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

Entity 2 Entity 2 non-polymer

Description description	GUANOSINE-5'-TRIPHOSPHATE
Molecular weight formula_weight	523.2 kDa
Source method src_method	syn
Copy count entity_count	10

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	185

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7. Fold Classification (SCOP + CATH) 30 domains

SCOP 2.08 (10 domains)

Domain ID domain_id	d1n3sa_
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	d1n3sb_
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	d1n3sc_
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	d1n3sd_
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	d1n3se_
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	d1n3sf_
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	d1n3sg_
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	d1n3sh_
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	d1n3si_
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	d1n3sj_
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 (20 domains)

Domain ID domain_id	1n3sA01
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	1n3sA02
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	1n3sB01
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	1n3sB02
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	1n3sC01
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	1n3sC02
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	1n3sD01
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	1n3sD02
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	1n3sE01
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	1n3sE02
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	1n3sF01
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	1n3sF02
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	1n3sG01
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	1n3sG02
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	1n3sH01
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	1n3sH02
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	1n3sI01
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	1n3sI02
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	1n3sJ01
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	1n3sJ02
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

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8. Citations (1)

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Unit-cell length a length_a	124.302 Å
Unit-cell length b length_b	124.302 Å
Unit-cell length c length_c	389.125 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	80

Space group space_group	P 43 21 2
Space-group number int_tables_number	96
Crystal system crystal_system	—

Resolution resolution	2.550 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.2710
R_work r_work	0.2620
R_free r_free	0.2930

fit	/app/data/saxs_computation/n3/1n3s/1n3s.fit
pddf	/app/data/pr_computation/n3/1n3s/1n3s.pr.out
profile	/app/data/saxs_computation/n3/1n3s/1n3s.dat