1a9c

GTP CYCLOHYDROLASE I (C110S MUTANT) IN COMPLEX WITH GTP

Method: X-RAY DIFFRACTION D_max: 237.0 Å Quality: GOOD

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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 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：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
2	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：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

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 1A9C	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 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 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
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 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 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 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 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：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 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：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 experimental conditions 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
1N3T 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 × 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 experimental conditions 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 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	1a9c
Deposition date deposition_date	1998-04-04
Structure title title	GTP CYCLOHYDROLASE I (C110S MUTANT) IN COMPLEX WITH GTP
Keywords keywords	HYDROLASE, GTP, PURINE HYDROLYSIS, PTERINE SYNTHESIS, TETRAHYDROBIOPTERIN; 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	80.43 Å
Radius of gyration Rg (electron density) rg_electron	81.61 Å
Forward intensity I(0) i0	2106290000.00
Molecular weight molecular_weight	377830.0 kDa
Excluded volume excluded_volume	469990 Å³
Envelope volume envelope_volume	855580 Å³
Hydration-shell volume shell_volume	95409 Å³
Envelope diameter envelope_diameter	280.2 Å
Shell Rg shell_rg	65.57 Å
Envelope Rg envelope_rg	79.45 Å
Shape Rg shape_rg	81.60 Å
Total Rg total_rg	81.37 Å
Total atoms total_atoms	32535
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	237.0 Å
Rg (real space) rg_real	80.02 Å
Rg uncertainty (real space) rg_real_error	1.54 Å
I(0) (real space) i0_real	2.0920e+09
I(0) uncertainty (real space) i0_real_error	3.9030e+07
Rg (reciprocal space) rg_reciprocal	76.87 Å
I(0) (reciprocal space) i0_reciprocal	2086000000.0000
Solution quality estimate total_estimate	0.8130
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	49.9 Å
Skewness Skewness skewness	0.435
Kurtosis Kurtosis kurtosis	-0.692
Angular range angular_range	— – 0.0950 Å⁻¹
Current regularization parameter α current_alpha	0.0449
Highest regularization parameter α highest_alpha	44330000.0000
Real-space data points n_real_points	20
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.904; Stabil: 0.991; Sysdev: 1.000; Positv: 1.000; Valcen: 0.841; Smooth: 0.009

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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	24717.4 kDa
EC 编号 ec_number	3.5.4.16
Mutation mutation	C110S
Source method src_method	man
Copy count entity_count	15

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K,L,M,N,O
Atom count atom_count	33165

PSLSKEAALVHEALVARGLETPLRPPVHEMDNETRKSLIAGHMTEIMQLLNLDLADDSLMETPHRIAKMYVDEIFSGLDYANFPKITLIENKMKVDEMVTVRDITLTSTSEHHFVTIDGKATVAYIPKDSVIGLSKINRIVQFFAQRPQVQERLTQQILIALQTLLGTNNVAVSIDAVHYCVKARGIRDATSATTTTSLGGLFKSSQNTRHEFLRAVRHHN

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	15

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	210

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7. Fold Classification (SCOP + CATH) 45 domains

SCOP 2.08 (15 domains)

Domain ID domain_id	d1a9ca_
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	d1a9cb_
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	d1a9cc_
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	d1a9cd_
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	d1a9ce_
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	d1a9cf_
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	d1a9cg_
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	d1a9ch_
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	d1a9ci_
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	d1a9cj_
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	d1a9ck_
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	d1a9cl_
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	d1a9cm_
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	d1a9cn_
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	d1a9co_
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	1a9cA01
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	1a9cA02
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	1a9cB01
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	1a9cB02
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	1a9cC01
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	1a9cC02
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	1a9cD01
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	1a9cD02
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	1a9cE01
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	1a9cE02
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	1a9cF01
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	1a9cF02
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	1a9cG01
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	1a9cG02
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	1a9cH01
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	1a9cH02
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	1a9cI01
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	1a9cI02
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	1a9cJ01
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	1a9cJ02
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	1a9cK01
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	1a9cK02
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	1a9cL01
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	1a9cL02
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	1a9cM01
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	1a9cM02
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	1a9cN01
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	1a9cN02
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	1a9cO01
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	1a9cO02
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 (5)

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Unit-cell length a length_a	313.900 Å
Unit-cell length b length_b	226.800 Å
Unit-cell length c length_c	131.400 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	2.900 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.2060
R_work r_work	0.2060
R_free r_free	0.2880