SAXSdb — 3qhy

▼

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

Beta-lactamase

Bacillus anthracis

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Beta-lactamase inhibitory protein II × 1 （O87916） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q93T42_BACAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–271； UniProt 39–309

Beta-lactamase inhibitory protein II

Streptomyces exfoliatus

UniProt O87916

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Beta-lactamase × 1 （Q93T42） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	O87916_STREX
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–271； UniProt 41–311

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	3qhy
Deposition date deposition_date	2011-01-26
Structure title title	Structural, thermodynamic and kinetic analysis of the picomolar binding affinity interaction of the beta-lactamase inhibitor protein-II (BLIP-II) with class A beta-lactamases
Keywords keywords	enyzme-inhibitor complex, beta-propeller, beta-lactamase, protein:protein interaction, HYDROLASE-HYDROLASE INHIBITOR complex; HYDROLASE/HYDROLASE INHIBITOR
Experimental Method method	X-RAY DIFFRACTION

▼

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.

3qhy__assembly_1__model_1

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

Download this curve (.dat)

3qhy__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3qhy__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	24.35 Å
Rg (electron density)	23.52 Å
Total Rg	24.47 Å
Atom count	3910
Residues	529
Excluded volume	68962 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3qhy__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Beta-lactamase
Molecular weight formula_weight	29759.6 kDa
EC 编号 ec_number	3.5.2.6
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	4418

KEKTGQVKHKNQATHKEFSQLEKKFDARLGVYAIDTGTNQTIAYRPNERFAFASTYKALAAGVLLQQNSTKKLDEVITYTKEDLVDYSPVTEKHVDTGMTLGEIAEAAVRYSDNTAGNILFHKIGGPKGYEKALRQMGDRVTMSDRFETELNEAIPGDIRDTSTAKAIATNLKAFTAGNALPNHKRNILTKWMKGNATGDKLIRAGVPTNWVVADKSGAGSYGTRNDIAIVWPPNRAPIIIAILSSKDEKGATYDNQLIAEAAEVIVNAFR

Source Source

Source organism organism	Bacillus anthracis
Common name common_name	anthrax,anthrax bacterium
NCBI taxonomy ID ncbi_taxonomy_id	1392
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Beta-lactamase inhibitory protein II
Molecular weight formula_weight	28360.9 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

ATSVVAWGGNNDWGEATVPAEAQSGVDAIAGGYFHGLALKGGKVLGWGANLNGQLTMPAATQSGVDAIAAGNYHSLALKDGEVIAWGGNEDGQTTVPAEARSGVDAIAAGAWASYALKDGKVIAWGDDSDGQTTVPAEAQSGVTALDGGVYTALAVKNGGVIAWGDNYFGQTTVPAEAQSGVDDVAGGIFHSLALKDGKVIAWGDNRYKQTTVPTEALSGVSAIASGEWYSLALKNGKVIAWGSSRTAPSSVQSGVSSIEAGPNAAYALKGGSGSGHHHHHH

Source Source

Source organism organism	Streptomyces exfoliatus
Common name common_name	Streptomyces hydrogenans
NCBI taxonomy ID ncbi_taxonomy_id	1905
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	508

▼

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d3qhya_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.3 — beta-lactamase/transpeptidase-like
Superfamily Superfamily superfamily	e.3.1 — beta-lactamase/transpeptidase-like
Family Family family	e.3.1.1 — beta-Lactamase/D-ala carboxypeptidase

Domain ID domain_id	d3qhyb_
Class class	b — All beta proteins
Fold Fold fold	b.69 — 7-bladed beta-propeller
Superfamily Superfamily superfamily	b.69.5 — RCC1/BLIP-II
Family Family family	b.69.5.2 — beta-lactamase inhibitor protein-II, BLIP-II

CATH v4.4 (2 domains)

Domain ID domain_id	3qhyA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	710 — Beta-lactamase
Homologous superfamily homologous superfamily	10 — DD-peptidase/beta-lactamase superfamily

Domain ID domain_id	3qhyB00
Class class	2 — Mainly Beta
Architecture architecture	130 — 7 Propeller
Topology topology	10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily	30 — Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II

▶

Unit-cell length a length_a	130.766 Å
Unit-cell length b length_b	87.177 Å
Unit-cell length c length_c	61.020 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	114.81 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.060 Å
Low-resolution limit resolution_low	49.950 Å
R factor r_factor	0.1720
R_work r_work	0.1690
R_free r_free	0.2170

Structural, thermodynamic and kinetic analysis of the picomolar binding affinity interaction of the beta-lactamase inhibitor protein-II (BLIP-II) with class A beta-lactamases

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

Beta-lactamase

State in the Current Structure

Other States of the Same Protein in the Database

Beta-lactamase inhibitory protein II

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

3qhy__assembly_1__model_1

3qhy__assembly_1__model_1 | I(q)

3qhy__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

Structural, thermodynamic and kinetic analysis of the picomolar binding affinity interaction of the beta-lactamase inhibitor protein-II (BLIP-II) with class A beta-lactamases

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

Beta-lactamase

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Beta-lactamase inhibitory protein II

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

3qhy__assembly_1__model_1

3qhy__assembly_1__model_1 | I(q)

3qhy__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)