SAXSdb — 2p0m

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

Arachidonate 15-lipoxygenase

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	FE (II) ION × 1 water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	FE (II) ION × 1 (2E)-3-(2-OCT-1-YN-1-YLPHENYL)ACRYLIC ACID × 1 water × 1	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 2	FE (II) ION × 2 (2E)-3-(2-OCT-1-YN-1-YLPHENYL)ACRYLIC ACID × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	LOX15_RABIT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–662； UniProt 2–663 Author chain B； PDBConstruct 1–662； UniProt 2–663

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	2p0m
Deposition date deposition_date	2007-02-28
Structure title title	Revised structure of rabbit reticulocyte 15S-lipoxygenase
Keywords keywords	rabbit, 15s-lipoxygenase, twin, pseudo symmetry, conformational change, arachidonate, iron, Oxidoreductase; OXIDOREDUCTASE
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.

2p0m__assembly_3__model_1

Assembly 3 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2p0m__assembly_3__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2p0m__assembly_3__model_1 | P(r) · Pending

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

Rg（Guinier）	40.32 Å
Rg (electron density)	40.17 Å
Total Rg	40.43 Å
Atom count	10613
Residues	1324
Excluded volume	190220 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2p0m__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2p0m__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`2p0m__assembly_3__model_1`	dimeric （2）	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	Arachidonate 15-lipoxygenase
Molecular weight formula_weight	75261.6 kDa
EC 编号 ec_number	1.13.11.33
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	10831

GVYRVCVSTGASIYAGSKNKVELWLVGQHGEVELGSCLRPTRNKEEEFKVNVSKYLGSLLFVRLRKKHFLKEDAWFCNWISVQALGAAEDKYWFPCYRWVVGDGVQSLPVGTGCTTVGDPQGLFQKHREQELEERRKLYQWGSWKEGLILNVAGSKLTDLPVDERFLEDKKIDFEASLAWGLAELALKNSLNILAPWKTLDDFNRIFWCGRSKLARRVRDSWQEDSLFGYQFLNGANPMLLRRSVQLPARLVFPPGMEELQAQLEKELKAGTLFEADFALLDNIKANVILYCQQYLAAPLVMLKLQPDGKLMPMVIQLHLPKIGSSPPPLFLPTDPPMVWLLAKCWVRSSDFQVHELNSHLLRGHLMAEVFTVATMRCLPSIHPVFKLIVPHLRYTLEINVRARNGLVSDFGIFDQIMSTGGGGHVQLLQQAGAFLTYRSFCPPDDLADRGLLGVESSFYAQDALRLWEIISRYVQGIMGLYYKTDEAVRDDLELQSWCREITEIGLQGAQKQGFPTSLQSVAQACHFVTMCIFTCTGQHSSIHLGQLDWFTWVPNAPCTMRLPPPTTKDATLETVMATLPNLHQSSLQMSIVWQLGRDQPIMVPLGQHQEEYFSGPEPRAVLEKFREELAIMDKEIEVRNEKLDIPYEYLRPSIVENSVAI

Entity 2 Entity 2 non-polymer

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

Entity 3 Entity 3 non-polymer

Description description	(2E)-3-(2-OCT-1-YN-1-YLPHENYL)ACRYLIC ACID
Molecular weight formula_weight	256.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	218

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6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d2p0ma1
Class class	a — All alpha proteins
Fold Fold fold	a.119 — Lipoxigenase
Superfamily Superfamily superfamily	a.119.1 — Lipoxigenase
Family Family family	a.119.1.2 — Animal lipoxigenases

Domain ID domain_id	d2p0ma2
Class class	b — All beta proteins
Fold Fold fold	b.12 — Lipase/lipooxygenase domain (PLAT/LH2 domain)
Superfamily Superfamily superfamily	b.12.1 — Lipase/lipooxygenase domain (PLAT/LH2 domain)
Family Family family	b.12.1.0 — automated matches

Domain ID domain_id	d2p0mb1
Class class	a — All alpha proteins
Fold Fold fold	a.119 — Lipoxigenase
Superfamily Superfamily superfamily	a.119.1 — Lipoxigenase
Family Family family	a.119.1.2 — Animal lipoxigenases

Domain ID domain_id	d2p0mb2
Class class	b — All beta proteins
Fold Fold fold	b.12 — Lipase/lipooxygenase domain (PLAT/LH2 domain)
Superfamily Superfamily superfamily	b.12.1 — Lipase/lipooxygenase domain (PLAT/LH2 domain)
Family Family family	b.12.1.0 — automated matches

CATH v4.4 (6 domains)

Domain ID domain_id	2p0mA01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	60 — Lipoxygenase-1
Homologous superfamily homologous superfamily	20 — PLAT/LH2 domain

Domain ID domain_id	2p0mA02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	245 — Lipoxygenase-1; domain 5
Homologous superfamily homologous superfamily	10 — Lipoxygenase-1; Domain 5

Domain ID domain_id	2p0mA03
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	60 —

Domain ID domain_id	2p0mB01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	60 — Lipoxygenase-1
Homologous superfamily homologous superfamily	20 — PLAT/LH2 domain

Domain ID domain_id	2p0mB02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	245 — Lipoxygenase-1; domain 5
Homologous superfamily homologous superfamily	10 — Lipoxygenase-1; Domain 5

Domain ID domain_id	2p0mB03
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	60 —

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Unit-cell length a length_a	198.900 Å
Unit-cell length b length_b	198.900 Å
Unit-cell length c length_c	136.100 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	18

Space group space_group	H 3
Space-group number int_tables_number	146
Crystal system crystal_system	—

Resolution resolution	2.400 Å
Low-resolution limit resolution_low	15.990 Å
R factor r_factor	0.1930
R_work r_work	0.1930
R_free r_free	0.2300

Revised structure of rabbit reticulocyte 15S-lipoxygenase

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

Arachidonate 15-lipoxygenase

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

2p0m__assembly_3__model_1

2p0m__assembly_3__model_1 | I(q)

2p0m__assembly_3__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

CATH v4.4 (6 domains)

7. Citations (2)

Revised structure of rabbit reticulocyte 15S-lipoxygenase

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

Arachidonate 15-lipoxygenase

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

2p0m__assembly_3__model_1

2p0m__assembly_3__model_1 | I(q)

2p0m__assembly_3__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

CATH v4.4 (6 domains)

7. Citations (2)