SAXSdb — 2pah

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

PROTEIN (PHENYLALANINE HYDROXYLASE)

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	FE (III) ION × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PH4H_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–335； UniProt 118–452 Author chain B； PDBConstruct 1–335； UniProt 118–452

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	2pah
Deposition date deposition_date	1998-05-26
Structure title title	TETRAMERIC HUMAN PHENYLALANINE HYDROXYLASE
Keywords keywords	HYDROXYLASE, PHENYLKETONURIA; HYDROXYLASE
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.

2pah__assembly_1__model_1

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

Download this curve (.dat)

2pah__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2pah__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	37.50 Å
Rg (electron density)	37.06 Å
Total Rg	37.41 Å
Atom count	10634
Residues	1302
Excluded volume	189980 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2pah__assembly_1__model_1`	tetrameric （4）	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 (2)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2paha_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.178 — Aromatic aminoacid monoxygenases, catalytic and oligomerization domains
Superfamily Superfamily superfamily	d.178.1 — Aromatic aminoacid monoxygenases, catalytic and oligomerization domains
Family Family family	d.178.1.1 — Aromatic aminoacid monoxygenases, catalytic and oligomerization domains

Domain ID domain_id	d2pahb_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.178 — Aromatic aminoacid monoxygenases, catalytic and oligomerization domains
Superfamily Superfamily superfamily	d.178.1 — Aromatic aminoacid monoxygenases, catalytic and oligomerization domains
Family Family family	d.178.1.1 — Aromatic aminoacid monoxygenases, catalytic and oligomerization domains

CATH v4.4 (2 domains)

Domain ID domain_id	2pahA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	800 — Phenylalanine Hydroxylase
Homologous superfamily homologous superfamily	10 — Aromatic amino acid hydroxylase

Domain ID domain_id	2pahB00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	800 — Phenylalanine Hydroxylase
Homologous superfamily homologous superfamily	10 — Aromatic amino acid hydroxylase

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Unit-cell length a length_a	119.500 Å
Unit-cell length b length_b	119.500 Å
Unit-cell length c length_c	126.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	P 31 1 2
Space-group number int_tables_number	151
Crystal system crystal_system	—

Resolution resolution	3.100 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.2510
R_work r_work	0.2510
R_free r_free	0.3260

Description description	PROTEIN (PHENYLALANINE HYDROXYLASE)
Molecular weight formula_weight	38641.9 kDa
EC 编号 ec_number	1.14.16.1
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	5317

TETRAMERIC HUMAN PHENYLALANINE HYDROXYLASE

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

PROTEIN (PHENYLALANINE HYDROXYLASE)

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

2pah__assembly_1__model_1

2pah__assembly_1__model_1 | I(q)

2pah__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli BL21

Description description	FE (III) ION
Molecular weight formula_weight	55.8 kDa
Source method src_method	syn
Copy count entity_count	2

TETRAMERIC HUMAN PHENYLALANINE HYDROXYLASE

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

PROTEIN (PHENYLALANINE HYDROXYLASE)

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

2pah__assembly_1__model_1

2pah__assembly_1__model_1 | I(q)

2pah__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)