SAXSdb — 1irm

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

apo heme oxygenase-1

Rattus norvegicus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count
3	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	HMOX1_RAT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–267； UniProt 1–267 Author chain B； PDBConstruct 1–267； UniProt 1–267 Author chain C； PDBConstruct 1–267； UniProt 1–267

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	1irm
Deposition date deposition_date	2001-10-09
Structure title title	Crystal structure of apo heme oxygenase-1
Keywords keywords	disordered alpha helix, apo form of hemoprotein, 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.

1irm__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1irm__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1irm__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	17.73 Å
Rg (electron density)	16.50 Å
Total Rg	17.64 Å
Atom count	1568
Residues	192
Excluded volume	27988 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1irm__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1irm__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1irm__assembly_3__model_1`	monomeric （1）	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) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1irma_
Class class	a — All alpha proteins
Fold Fold fold	a.132 — Heme oxygenase-like
Superfamily Superfamily superfamily	a.132.1 — Heme oxygenase-like
Family Family family	a.132.1.1 — Eukaryotic type heme oxygenase

Domain ID domain_id	d1irmb_
Class class	a — All alpha proteins
Fold Fold fold	a.132 — Heme oxygenase-like
Superfamily Superfamily superfamily	a.132.1 — Heme oxygenase-like
Family Family family	a.132.1.1 — Eukaryotic type heme oxygenase

Domain ID domain_id	d1irmc_
Class class	a — All alpha proteins
Fold Fold fold	a.132 — Heme oxygenase-like
Superfamily Superfamily superfamily	a.132.1 — Heme oxygenase-like
Family Family family	a.132.1.1 — Eukaryotic type heme oxygenase

CATH v4.4 (3 domains)

Domain ID domain_id	1irmA00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	910 — Heme Oxygenase; Chain A
Homologous superfamily homologous superfamily	10 — Heme oxygenase-like

Domain ID domain_id	1irmB00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	910 — Heme Oxygenase; Chain A
Homologous superfamily homologous superfamily	10 — Heme oxygenase-like

Domain ID domain_id	1irmC00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	910 — Heme Oxygenase; Chain A
Homologous superfamily homologous superfamily	10 — Heme oxygenase-like

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Unit-cell length a length_a	70.210 Å
Unit-cell length b length_b	70.210 Å
Unit-cell length c length_c	140.460 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	9

Space group space_group	P 32
Space-group number int_tables_number	145
Crystal system crystal_system	—

Resolution resolution	2.550 Å
Low-resolution limit resolution_low	46.625 Å
R factor r_factor	0.2040
R_work r_work	0.2024
R_free r_free	0.3068

Description description	apo heme oxygenase-1
Molecular weight formula_weight	30612.5 kDa
EC 编号 ec_number	1.14.99.3
Source method src_method	man
Copy count entity_count	3

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,A,B
Atom count atom_count	4836

Crystal structure of apo heme oxygenase-1

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

apo heme oxygenase-1

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

1irm__assembly_2__model_1

1irm__assembly_2__model_1 | I(q)

1irm__assembly_2__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) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

7. Citations (3)

Source organism organism	Rattus norvegicus
Common name common_name	Norway rat
NCBI taxonomy ID ncbi_taxonomy_id	10116
Host organism host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	87

Crystal structure of apo heme oxygenase-1

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

apo heme oxygenase-1

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

1irm__assembly_2__model_1

1irm__assembly_2__model_1 | I(q)

1irm__assembly_2__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) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

7. Citations (3)