SAXSdb — 2or0

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

Hydroxylase

Rhodococcus sp.

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	ACETATE ION × 6 water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	ACETATE ION × 6 water × 1	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 4	ACETATE ION × 24 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q0S6I7_RHOSR
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 22–412； UniProt 1–391 Author chain B； PDBConstruct 22–412； UniProt 1–391

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	2or0
Deposition date deposition_date	2007-02-01
Structure title title	Structural Genomics, the crystal structure of a putative hydroxylase from Rhodococcus sp. RHA1
Keywords keywords	;APC7385, putative hydroxylase, Rhodococcus sp. RHA1, structural genomics, PSI-2, protein structure initiative, midwest center for structural genomics, MCSG, 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.

2or0__assembly_2__model_1

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

Download this curve (.dat)

2or0__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2or0__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	22.52 Å
Rg (electron density)	21.59 Å
Total Rg	22.40 Å
Atom count	3136
Residues	397
Excluded volume	55301 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2or0__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2or0__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`2or0__assembly_3__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 (3)

Entity 1 Entity 1 polymer

Description description	Hydroxylase
Molecular weight formula_weight	45287.9 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	6682

MGSSHHHHHHSSGRENLYFQGMGRVLDRIEVVAEEIRGQAVQSEADCRLTDAAAGLLRDSGAIRLLQPRLYGGYEVHPREFAETVMGVAALDGASGWVTGIVGVHPWELAFADPQVQEEIWGEDNDTWMASPYAPMGVATPVDGGYVLKGRWSFSSGTDHCQWAFLGAMVGDGEGGIATPSSLHVILPRTDYQIVEDTWDVIGLRGTGSKDLIVDGAFVPGYRTLNAAKVMDGRAQKEAGRPEPLFNMPYSCMFPLGITAAVIGITEGALACHIAVQKDRVAITGQKIKEDPYVLSAIGESAAEINASRVSLIETADRFYDKVDAGKEITFEERAIGRRTQIAAAWRAVRAADEIFARAGGGALHYKTPMQRFWRDAHAGLAHAVHVPGPTNHASALTQLGGEPQGMMRAMIGS

Source Source

Source organism organism	Rhodococcus sp.
NCBI taxonomy ID ncbi_taxonomy_id	101510
Host organism host_organism	Escherichia coli BL21

Entity 2 Entity 2 non-polymer

Description description	ACETATE ION
Molecular weight formula_weight	59.0 kDa
Source method src_method	syn
Copy count entity_count	12

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	559

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6. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id	2or0A01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	540 — Butyryl-Coa Dehydrogenase, subunit A; domain 1
Homologous superfamily homologous superfamily	10 — Acyl-CoA dehydrogenase/oxidase, N-terminal domain

Domain ID domain_id	2or0A02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	110 — Butyryl-CoA Dehydrogenase, subunit A; domain 2
Homologous superfamily homologous superfamily	10 — Butyryl-CoA Dehydrogenase, subunit A, domain 2

Domain ID domain_id	2or0A03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily	10 — Butyryl-CoA Dehydrogenase, subunit A, domain 3

Domain ID domain_id	2or0B01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	540 — Butyryl-Coa Dehydrogenase, subunit A; domain 1
Homologous superfamily homologous superfamily	10 — Acyl-CoA dehydrogenase/oxidase, N-terminal domain

Domain ID domain_id	2or0B02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	110 — Butyryl-CoA Dehydrogenase, subunit A; domain 2
Homologous superfamily homologous superfamily	10 — Butyryl-CoA Dehydrogenase, subunit A, domain 2

Domain ID domain_id	2or0B03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily	10 — Butyryl-CoA Dehydrogenase, subunit A, domain 3

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Unit-cell length a length_a	99.881 Å
Unit-cell length b length_b	99.881 Å
Unit-cell length c length_c	407.920 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	24

Space group space_group	P 65 2 2
Space-group number int_tables_number	179
Crystal system crystal_system	—

Resolution resolution	2.100 Å
Low-resolution limit resolution_low	34.730 Å
R factor r_factor	0.1855
R_work r_work	0.1838
R_free r_free	0.2176

Structural Genomics, the crystal structure of a putative hydroxylase from Rhodococcus sp. RHA1

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

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

2or0__assembly_2__model_1

2or0__assembly_2__model_1 | I(q)

2or0__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

7. Citations (1)

Structural Genomics, the crystal structure of a putative hydroxylase from Rhodococcus sp. RHA1

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

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

2or0__assembly_2__model_1

2or0__assembly_2__model_1 | I(q)

2or0__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

7. Citations (1)