SAXSdb — 3gmv

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

Beta-lactamase inhibitory protein BLIP-I

Streptomyces exfoliatus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	TRIS(HYDROXYETHYL)AMINOMETHANE × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9KJ90_STREX
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain X； PDBConstruct 1–156； UniProt 31–186

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	3gmv
Deposition date deposition_date	2009-03-15
Structure title title	Crystal Structure of Beta-Lactamse Inhibitory Protein-I (BLIP-I) in Apo Form
Keywords keywords	2-layer alpha/beta sandwich, PROTEIN BINDING; PROTEIN BINDING
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.

3gmv__assembly_1__model_1

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

Download this curve (.dat)

3gmv__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3gmv__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	17.20 Å
Rg (electron density)	16.21 Å
Total Rg	17.24 Å
Atom count	1226
Residues	156
Excluded volume	21594 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3gmv__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 (3)

Entity 1 Entity 1 polymer

Description description	Beta-lactamase inhibitory protein BLIP-I
Molecular weight formula_weight	17219.0 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	X
Atom count atom_count	1433

SGFSAEKYEQIQFGMTFDEVWEIGGGEAACDTGGVIGDSILCFTESGDYAPYGGFSFTDEGELWSKRNEYLYKAKTPSVKLSHYNRTALGMTEAQLWAAVPKDSCVSQGESYPNWPAKTGFEEKYYCAAATGLFPPSASFHLTDGVLTYRYQRSLT

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 2 Entity 2 non-polymer

Description description	TRIS(HYDROXYETHYL)AMINOMETHANE
Molecular weight formula_weight	163.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	201

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d3gmvx_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.98 — BLIP-like
Superfamily Superfamily superfamily	d.98.1 — beta-lactamase-inhibitor protein, BLIP
Family Family family	d.98.1.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id	3gmvX00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	730 — BLIP domain

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Unit-cell length a length_a	98.735 Å
Unit-cell length b length_b	44.071 Å
Unit-cell length c length_c	45.291 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	104.58 °
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	1.800 Å
Low-resolution limit resolution_low	20.490 Å
R factor r_factor	0.1874
R_work r_work	0.1854
R_free r_free	0.2270

Crystal Structure of Beta-Lactamse Inhibitory Protein-I (BLIP-I) in Apo Form

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

Beta-lactamase inhibitory protein BLIP-I

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

3gmv__assembly_1__model_1

3gmv__assembly_1__model_1 | I(q)

3gmv__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 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)

Crystal Structure of Beta-Lactamse Inhibitory Protein-I (BLIP-I) in Apo Form

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

Beta-lactamase inhibitory protein BLIP-I

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

3gmv__assembly_1__model_1

3gmv__assembly_1__model_1 | I(q)

3gmv__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 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)