SAXSdb — 1qto

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

BLEOMYCIN-BINDING PROTEIN

Streptomyces verticillus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q53793_9ACTO
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–122； UniProt 1–122

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	1qto
Deposition date deposition_date	1999-06-28
Structure title title	1.5 A CRYSTAL STRUCTURE OF A BLEOMYCIN RESISTANCE DETERMINANT FROM BLEOMYCIN-PRODUCING STREPTOMYCES VERTICILLUS
Keywords keywords	ARM-EXCHANGE, ANTIBIOTIC INHIBITOR; ANTIBIOTIC INHIBITOR
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.

1qto__assembly_1__model_1

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

Download this curve (.dat)

1qto__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1qto__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	18.87 Å
Rg (electron density)	17.56 Å
Total Rg	18.55 Å
Atom count	1868
Residues	244
Excluded volume	32601 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1qto__assembly_1__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 (2)

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1qtoa_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.32 — Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
Superfamily Superfamily superfamily	d.32.1 — Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
Family Family family	d.32.1.2 — Antibiotic resistance proteins

CATH v4.4 (1 domains)

Domain ID domain_id	1qtoA00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	180 — 2,3-Dihydroxybiphenyl 1,2-Dioxygenase; domain 1
Homologous superfamily homologous superfamily	10 — 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1

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7. Citations (6)

The 1.5 A crystal structure of a bleomycin resistance determinant from bleomycin-producing Streptomyces verticillus.

J.Mol.Biol. (2000)

PMID: 10656800 · DOI: 10.1006/jmbi.1999.3404 PRIMARY

Characterization of the bleomycin resistance determinant encoded on the transposon Tn5

FEBS Lett. (1999)

DOI: 10.1016/S0014-5793(98)01613-5

Mutation of the N-terminal proline 9 of BLMA from Streptomyces verticillus abolishes the binding affinity for bleomycin

FEBS Lett. (1999)

DOI: 10.1016/S0014-5793(99)00478-0

;Crystallization and preliminary X-ray diffraction studies of bleomycin-binding protein from bleomycin-producing Streptomyces verticillus ;

Acta Crystallogr.,Sect.D (1998)

DOI: 10.1107/S0907444997008871

;Overproduction of the bleomycin-binding proteins from bleomycin-producing Streptomyces verticillus and a methicillin-resistant Staphylococcus aureus in Escherichia coli and their immunological characterisation ;

FEBS Lett. (1995)

DOI: 10.1016/0014-5793(95)00218-X

Characterisation by molecular cloning of two genes from Streptomyces verticillus encoding resistance to bleomycin

Gene (1994)

DOI: 10.1016/0378-1119(94)90626-2

Unit-cell length a length_a	54.940 Å
Unit-cell length b length_b	67.880 Å
Unit-cell length c length_c	35.610 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	4

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	1.500 Å
Low-resolution limit resolution_low	10.000 Å
R factor r_factor	—
R_work r_work	0.1900
R_free r_free	0.2210

Description description	BLEOMYCIN-BINDING PROTEIN
Molecular weight formula_weight	13243.6 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1025

1.5 A CRYSTAL STRUCTURE OF A BLEOMYCIN RESISTANCE DETERMINANT FROM BLEOMYCIN-PRODUCING STREPTOMYCES VERTICILLUS

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

BLEOMYCIN-BINDING PROTEIN

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

1qto__assembly_1__model_1

1qto__assembly_1__model_1 | I(q)

1qto__assembly_1__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (6)

Source organism organism	Streptomyces verticillus
NCBI taxonomy ID ncbi_taxonomy_id	29309
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	91

1.5 A CRYSTAL STRUCTURE OF A BLEOMYCIN RESISTANCE DETERMINANT FROM BLEOMYCIN-PRODUCING STREPTOMYCES VERTICILLUS

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

BLEOMYCIN-BINDING PROTEIN

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

1qto__assembly_1__model_1

1qto__assembly_1__model_1 | I(q)

1qto__assembly_1__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (6)