SAXSdb — 7al9

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

GTP cyclohydrolase 1 feedback regulatory protein

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 5	POTASSIUM ION × 5 PHENYLALANINE × 5 water × 5	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 5	POTASSIUM ION × 5 PHENYLALANINE × 5 water × 5	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	GFRP_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–87； UniProt 1–84 Author chain B； PDBConstruct 4–87； UniProt 1–84 Author chain C； PDBConstruct 4–87； UniProt 1–84 Author chain D； PDBConstruct 4–87； UniProt 1–84 Author chain E； PDBConstruct 4–87； UniProt 1–84 Author chain F； PDBConstruct 4–87； UniProt 1–84 Author chain G； PDBConstruct 4–87； UniProt 1–84 Author chain H； PDBConstruct 4–87； UniProt 1–84 Author chain I； PDBConstruct 4–87； UniProt 1–84 Author chain J； PDBConstruct 4–87； UniProt 1–84

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	7al9
Deposition date deposition_date	2020-10-06
Structure title title	human GTP cyclohydrolase I feedback regulatory protein (GFRP) in complex with phenylalanine
Keywords keywords	;GTP cyclohydrolase 1 feedback regulatory protein, regulatory protein, L-phenylalanine binding (Phe) synthesis allosteric regulation, PROTEIN BINDING ;; PROTEIN BINDING
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

7al9__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

7al9__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

7al9__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	23.18 Å
Rg (electron density)	21.82 Å
Total Rg	22.56 Å
Atom count	3468
Residues	415
Excluded volume	61285 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`7al9__assembly_1__model_1`	pentameric （5）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`7al9__assembly_2__model_1`	pentameric （5）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	GTP cyclohydrolase 1 feedback regulatory protein
Molecular weight formula_weight	9992.5 kDa
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	7289

GSHMPYLLISTQIRMEVGPTMVGDEQSDPELMQHLGASKRRALGNNFYEYYVDDPPRIVLDKLERRGFRVLSMTGVGQTLVWCLHKE

Source Source

Source organism organism	Homo sapiens
Common name common_name	Human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	POTASSIUM ION
Molecular weight formula_weight	39.1 kDa
Source method src_method	syn
Copy count entity_count	10

Entity 3 Entity 3 non-polymer

Description description	PHENYLALANINE
Molecular weight formula_weight	165.2 kDa
Source method src_method	nat
Copy count entity_count	10

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	349

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Unit-cell length a length_a	66.939 Å
Unit-cell length b length_b	98.123 Å
Unit-cell length c length_c	67.455 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	102.53 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	20

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.745 Å
Low-resolution limit resolution_low	54.680 Å
R factor r_factor	0.2045
R_work r_work	0.2029
R_free r_free	0.2346

human GTP cyclohydrolase I feedback regulatory protein (GFRP) in complex with phenylalanine

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

GTP cyclohydrolase 1 feedback regulatory protein

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

7al9__assembly_1__model_1

7al9__assembly_1__model_1 | I(q)

7al9__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

7. Citations (1)

human GTP cyclohydrolase I feedback regulatory protein (GFRP) in complex with phenylalanine

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

GTP cyclohydrolase 1 feedback regulatory protein

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

7al9__assembly_1__model_1

7al9__assembly_1__model_1 | I(q)

7al9__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

7. Citations (1)