1y2m

Crystal structure of phenylalanine ammonia-lyase from yeast Rhododporidium toruloides

Method: X-RAY DIFFRACTION

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

Phenylalanine ammonia-lyase

Rhodosporidium toruloides

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PALY_RHOTO
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–716； UniProt 1–716 Author chain B； PDBConstruct 1–716； UniProt 1–716 Author chain C； PDBConstruct 1–716； UniProt 1–716 Author chain D； PDBConstruct 1–716； UniProt 1–716

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	1y2m
Deposition date deposition_date	2004-11-22
Structure title title	Crystal structure of phenylalanine ammonia-lyase from yeast Rhododporidium toruloides
Keywords keywords	Alpha helices, LYASE; LYASE
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.

1y2m__assembly_1__model_1

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

Download this curve (.dat)

1y2m__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1y2m__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	40.14 Å
Rg (electron density)	39.65 Å
Total Rg	39.89 Å
Atom count	20155
Residues	2606
Excluded volume	359980 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1y2m__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)

Entity 1 Entity 1 polymer

Description description	Phenylalanine ammonia-lyase
Molecular weight formula_weight	77672.9 kDa
EC 编号 ec_number	4.3.1.5
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	22123

MAPSLDSISHSFANGVASAKQAVNGASTNLAVAGSHLPTTQVTQVDIVEKMLAAPTDSTLELDGYSLNLGDVVSAARKGRPVRVKDSDEIRSKIDKSVEFLRSQLSMSVYGVTTGFGGSADTRTEDAISLQKALLEHQLCGVLPSSFDSFRLGRGLENSLPLEVVRGAMTIRVNSLTRGHSAVRLVVLEALTNFLNHGITPIVPLRGTISASGDLSPLSYIAAAISGHPDSKVHVVHEGKEKILYAREAMALFNLEPVVLGPKEGLGLVNGTAVSASMATLALHDAHMLSLLSQSLTAMTVEAMVGHAGSFHPFLHDVTRPHPTQIEVAGNIRKLLEGSRFAVHHEEEVKVKDDEGILRQDRYPLRTSPQWLGPLVSDLIHAHAVLTIEAGQSTTDNPLIDVENKTSHHGGNFQAAAVANTMEKTRLGLAQIGKLNFTQLTEMLNAGMNRGLPSCLAAEDPSLSYHCKGLDIAAAAYTSELGHLANPVTTHVQPAEMANQAVNSLALISARRTTESNDVLSLLLATHLYCVLQAIDLRAIEFEFKKQFGPAIVSLIDQHFGSAMTGSNLRDELVEKVNKTLAKRLEQTNSYDLVPRWHDAFSFAAGTVVEVLSSTSLSLAAVNAWKVAAAESAISLTRQVRETFWSAASTSSPALSYLSPRTQILYAFVREELGVKARRGDVFLGKQEVTIGSNVSKIYEAIKSGRINNVLLKMLA

Source Source

Source organism organism	Rhodosporidium toruloides
NCBI taxonomy ID ncbi_taxonomy_id	5286
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1915

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6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1y2ma_
Class class	a — All alpha proteins
Fold Fold fold	a.127 — L-aspartase-like
Superfamily Superfamily superfamily	a.127.1 — L-aspartase-like
Family Family family	a.127.1.2 — HAL/PAL-like

Domain ID domain_id	d1y2mb_
Class class	a — All alpha proteins
Fold Fold fold	a.127 — L-aspartase-like
Superfamily Superfamily superfamily	a.127.1 — L-aspartase-like
Family Family family	a.127.1.2 — HAL/PAL-like

Domain ID domain_id	d1y2mc_
Class class	a — All alpha proteins
Fold Fold fold	a.127 — L-aspartase-like
Superfamily Superfamily superfamily	a.127.1 — L-aspartase-like
Family Family family	a.127.1.2 — HAL/PAL-like

Domain ID domain_id	d1y2md_
Class class	a — All alpha proteins
Fold Fold fold	a.127 — L-aspartase-like
Superfamily Superfamily superfamily	a.127.1 — L-aspartase-like
Family Family family	a.127.1.2 — HAL/PAL-like

CATH v4.4 (12 domains)

Domain ID domain_id	1y2mA01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	275 — Fumarase C; Chain B, domain 1
Homologous superfamily homologous superfamily	10 — Fumarase/aspartase (N-terminal domain)

Domain ID domain_id	1y2mA02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	200 — Fumarase C; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Fumarase/aspartase (Central domain)

Domain ID domain_id	1y2mA03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	274 — Enzyme I; Chain A, domain 2
Homologous superfamily homologous superfamily	20 — Phenylalanine ammonia-lyase 1; domain 3

Domain ID domain_id	1y2mB01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	275 — Fumarase C; Chain B, domain 1
Homologous superfamily homologous superfamily	10 — Fumarase/aspartase (N-terminal domain)

Domain ID domain_id	1y2mB02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	200 — Fumarase C; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Fumarase/aspartase (Central domain)

Domain ID domain_id	1y2mB03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	274 — Enzyme I; Chain A, domain 2
Homologous superfamily homologous superfamily	20 — Phenylalanine ammonia-lyase 1; domain 3

Domain ID domain_id	1y2mC01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	275 — Fumarase C; Chain B, domain 1
Homologous superfamily homologous superfamily	10 — Fumarase/aspartase (N-terminal domain)

Domain ID domain_id	1y2mC02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	200 — Fumarase C; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Fumarase/aspartase (Central domain)

Domain ID domain_id	1y2mC03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	274 — Enzyme I; Chain A, domain 2
Homologous superfamily homologous superfamily	20 — Phenylalanine ammonia-lyase 1; domain 3

Domain ID domain_id	1y2mD01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	275 — Fumarase C; Chain B, domain 1
Homologous superfamily homologous superfamily	10 — Fumarase/aspartase (N-terminal domain)

Domain ID domain_id	1y2mD02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	200 — Fumarase C; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Fumarase/aspartase (Central domain)

Domain ID domain_id	1y2mD03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	274 — Enzyme I; Chain A, domain 2
Homologous superfamily homologous superfamily	20 — Phenylalanine ammonia-lyase 1; domain 3

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Unit-cell length a length_a	104.759 Å
Unit-cell length b length_b	151.612 Å
Unit-cell length c length_c	179.922 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	16

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	1.600 Å
Low-resolution limit resolution_low	41.880 Å
R factor r_factor	0.1593
R_work r_work	0.1579
R_free r_free	0.1865

Crystal structure of phenylalanine ammonia-lyase from yeast Rhododporidium toruloides

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

Phenylalanine ammonia-lyase

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

1y2m__assembly_1__model_1

1y2m__assembly_1__model_1 | I(q)

1y2m__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 water

6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (4 domains)

CATH v4.4 (12 domains)

7. Citations (2)

Crystal structure of phenylalanine ammonia-lyase from yeast Rhododporidium toruloides

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

Phenylalanine ammonia-lyase

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

1y2m__assembly_1__model_1

1y2m__assembly_1__model_1 | I(q)

1y2m__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 water

6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (4 domains)

CATH v4.4 (12 domains)

7. Citations (2)