SAXSdb — 1k9b

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

BOWMAN-BIRK TYPE PROTEINASE INHIBITOR

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	water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	IBB1_SOYBN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–58； UniProt 45–102

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	1k9b
Deposition date deposition_date	2001-10-29
Structure title title	Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28 nm resolution. Structural peculiarities in a folded protein conformation
Keywords keywords	TRIPPLE-STRANDED BETA HAIRPIN, DOUBLE-HEADED, HYDROLASE INHIBITOR; HYDROLASE 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.

1k9b__assembly_1__model_1

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

Download this curve (.dat)

1k9b__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1k9b__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	12.32 Å
Rg (electron density)	11.95 Å
Total Rg	12.82 Å
Atom count	513
Residues	58
Excluded volume	7315 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1k9b__assembly_1__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) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1k9ba_
Class class	g — Small proteins
Fold Fold fold	g.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamily	g.3.13 — Bowman-Birk inhibitor, BBI
Family Family family	g.3.13.1 — Bowman-Birk inhibitor, BBI

CATH v4.4 (1 domains)

Domain ID domain_id	1k9bA00
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	69 — Cysteine Protease (Bromelain) Inhibitor, subunit H
Homologous superfamily homologous superfamily	10 — Cysteine Protease (Bromelain) Inhibitor, subunit H

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7. Citations (6)

;Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution. Structural peculiarities in a folded protein conformation. ;

Eur.J.Biochem. (1996)

PMID: 8954162 · DOI: 10.1111/j.1432-1033.1996.0122r.x PRIMARY

;Crystal Structure of Cancer Chemopreventive Bowman-Birk Inhibitor in Ternary Complex with Bovine Trypsin at 2.3 Ao Resolution. Structural Basis of Janus-faced Serine Protease Inhibitor Specificity ;

J.Mol.Biol. (2000)

DOI: 10.1006/jmbi.2000.3677

;Mutational analysis of disulfide bonds in the trypsin-reactive subdomain of a Bowman-Birk-type inhibitor of trypsin and chymotrypsin. Cooperative versus autonomous refolding of subdomains ;

Eur.J.Biochem. (1998)

DOI: 10.1046/j.1432-1327.1998.2510854.x

Template-directed protein folding into a metastable state of increased activity

Eur.J.Biochem. (1995)

;A new and general procedure for refolding mutant Bowman-Birk-type proteinase inhibitors on trypsin-Sepharose as a matrix with complementary structure. ;

FEBS Lett. (1989)

DOI: 10.1016/0014-5793(89)80909-3

Chemical synthesis, molecular cloning and expression of gene coding for a Bowman-Birk-type proteinase inhibitor

Eur.J.Biochem. (1987)

Unit-cell length a length_a	86.100 Å
Unit-cell length b length_b	86.100 Å
Unit-cell length c length_c	86.100 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	24

Space group space_group	P 41 3 2
Space-group number int_tables_number	213
Crystal system crystal_system	—

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	—
R_work r_work	0.2210
R_free r_free	0.3080

Description description	BOWMAN-BIRK TYPE PROTEINASE INHIBITOR
Molecular weight formula_weight	6431.5 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	530

Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28 nm resolution. Structural peculiarities in a folded protein conformation

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

BOWMAN-BIRK TYPE PROTEINASE INHIBITOR

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

1k9b__assembly_1__model_1

1k9b__assembly_1__model_1 | I(q)

1k9b__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

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)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	17

Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28 nm resolution. Structural peculiarities in a folded protein conformation

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

BOWMAN-BIRK TYPE PROTEINASE INHIBITOR

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

1k9b__assembly_1__model_1

1k9b__assembly_1__model_1 | I(q)

1k9b__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

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)