1fbx

CRYSTAL STRUCTURE OF ZINC-CONTAINING E.COLI GTP CYCLOHYDROLASE I

Method: X-RAY DIFFRACTION D_max: 533.0 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 A； UniProt 2–222 Chain B； UniProt 2–222 Chain C； UniProt 2–222 Chain D； UniProt 2–222 Chain E； UniProt 2–222	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
2	Protein homooligomer Homooligomer Protein × 10 PDB declaration: decameric（10） Consistent with protein copy count	Chain F； UniProt 2–222 Chain G； UniProt 2–222 Chain H； UniProt 2–222 Chain I； UniProt 2–222 Chain J； UniProt 2–222 Chain K； UniProt 2–222 Chain L； UniProt 2–222 Chain M； UniProt 2–222 Chain N； UniProt 2–222 Chain O； UniProt 2–222	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

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 1FBX	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 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 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 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 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 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 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 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 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
1GTP GTP CYCLOHYDROLASE I Deposited 1995-09-16	Different construct 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 construct 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 construct 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 construct 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 construct 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 construct Different mutation/modification Different ligand/ion 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 construct Different mutation/modification Different ligand/ion 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 construct 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 construct 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 construct Different mutation/modification Different ligand/ion 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 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 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 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 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 2–222 Author chain B； PDBConstruct 1–221； UniProt 2–222 Author chain C； PDBConstruct 1–221； UniProt 2–222 Author chain D； PDBConstruct 1–221； UniProt 2–222 Author chain E； PDBConstruct 1–221； UniProt 2–222 Author chain F； PDBConstruct 1–221； UniProt 2–222 Author chain G； PDBConstruct 1–221； UniProt 2–222 Author chain H； PDBConstruct 1–221； UniProt 2–222 Author chain I； PDBConstruct 1–221； UniProt 2–222 Author chain J； PDBConstruct 1–221； UniProt 2–222 Author chain K； PDBConstruct 1–221； UniProt 2–222 Author chain L； PDBConstruct 1–221； UniProt 2–222 Author chain M； PDBConstruct 1–221； UniProt 2–222 Author chain N； PDBConstruct 1–221； UniProt 2–222 Author chain O； PDBConstruct 1–221； UniProt 2–222

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	1fbx
Deposition date deposition_date	2000-07-17
Structure title title	CRYSTAL STRUCTURE OF ZINC-CONTAINING E.COLI GTP CYCLOHYDROLASE I
Keywords keywords	HYDROLASE, ALLOSTERIC ENZYME; 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	— Å
Radius of gyration Rg (electron density) rg_electron	125.80 Å
Forward intensity I(0) i0	1910180000.00
Molecular weight molecular_weight	371730.0 kDa
Excluded volume excluded_volume	464930 Å³
Envelope volume envelope_volume	958950 Å³
Hydration-shell volume shell_volume	63668 Å³
Envelope diameter envelope_diameter	367.9 Å
Shell Rg shell_rg	119.40 Å
Envelope Rg envelope_rg	124.00 Å
Shape Rg shape_rg	125.80 Å
Total Rg total_rg	125.80 Å
Total atoms total_atoms	26010
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	533.0 Å
Rg (real space) rg_real	124.70 Å
Rg uncertainty (real space) rg_real_error	15.48 Å
I(0) (real space) i0_real	1.9090e+09
I(0) uncertainty (real space) i0_real_error	5.8440e+07
Rg (reciprocal space) rg_reciprocal	83.57 Å
I(0) (reciprocal space) i0_reciprocal	1692000000.0000
Solution quality estimate total_estimate	0.5539
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	4
Primary peak position r_peak_primary	44.4 Å
Skewness Skewness skewness	0.176
Kurtosis Kurtosis kurtosis	-2.420
Angular range angular_range	— – 0.0600 Å⁻¹
Current regularization parameter α current_alpha	0.0568
Highest regularization parameter α highest_alpha	18170000.0000
Real-space data points n_real_points	13
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.002; Oscil: 0.000; Stabil: 0.747; Sysdev: 1.000; Positv: 1.000; Valcen: 0.000; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	GTP CYCLOHYDROLASE I
Molecular weight formula_weight	24733.5 kDa
EC 编号 ec_number	3.5.4.16
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	26025

PSLSKEAALVHEALVARGLETPLRPPVHEMDNETRKSLIAGHMTEIMQLLNLDLADDSLMETPHRIAKMYVDEIFSGLDYANFPKITLIENKMKVDEMVTVRDITLTSTCEHHFVTIDGKATVAYIPKDSVIGLSKINRIVQFFAQRPQVQERLTQQILIALQTLLGTNNVAVSIDAVHYCVKARGIRDATSATTTTSLGGLFKSSQNTRHEFLRAVRHHN

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	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	15

Entity 3 Entity 3 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	15

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	15

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7. Fold Classification (SCOP + CATH) 45 domains

SCOP 2.08 (15 domains)

Domain ID domain_id	d1fbxa_
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	d1fbxb_
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	d1fbxc_
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	d1fbxd_
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	d1fbxe_
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	d1fbxf_
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	d1fbxg_
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	d1fbxh_
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	d1fbxi_
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	d1fbxj_
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	d1fbxk_
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	d1fbxl_
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	d1fbxm_
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	d1fbxn_
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	d1fbxo_
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	1fbxA01
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	1fbxA02
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	1fbxB01
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	1fbxB02
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	1fbxC01
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	1fbxC02
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	1fbxD01
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	1fbxD02
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	1fbxE01
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	1fbxE02
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	1fbxF01
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	1fbxF02
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	1fbxG01
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	1fbxG02
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	1fbxH01
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	1fbxH02
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	1fbxI01
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	1fbxI02
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	1fbxJ01
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	1fbxJ02
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	1fbxK01
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	1fbxK02
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	1fbxL01
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	1fbxL02
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	1fbxM01
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	1fbxM02
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	1fbxN01
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	1fbxN02
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	1fbxO01
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	1fbxO02
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	227.690 Å
Unit-cell length b length_b	314.190 Å
Unit-cell length c length_c	132.570 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	2.800 Å
Low-resolution limit resolution_low	14.980 Å
R factor r_factor	0.2020
R_work r_work	0.2020
R_free r_free	0.2510