SAXSdb — 9u5s

▼

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

Outer membrane lipoprotein BfpB

Escherichia coli O127:H6 str. E2348/69

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 34	Lipoprotein × 17 （B7UTD2）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	BFPB_ECO27
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–535； UniProt 18–552 Author chain B； PDBConstruct 1–535； UniProt 18–552 Author chain C； PDBConstruct 1–535； UniProt 18–552 Author chain D； PDBConstruct 1–535； UniProt 18–552 Author chain E； PDBConstruct 1–535； UniProt 18–552 Author chain F； PDBConstruct 1–535； UniProt 18–552 Author chain G； PDBConstruct 1–535； UniProt 18–552 Author chain H； PDBConstruct 1–535； UniProt 18–552 Author chain I； PDBConstruct 1–535； UniProt 18–552 Author chain J； PDBConstruct 1–535； UniProt 18–552 Author chain K； PDBConstruct 1–535； UniProt 18–552 Author chain L； PDBConstruct 1–535； UniProt 18–552 Author chain M； PDBConstruct 1–535； UniProt 18–552 Author chain N； PDBConstruct 1–535； UniProt 18–552 Author chain O； PDBConstruct 1–535； UniProt 18–552 Author chain P； PDBConstruct 1–535； UniProt 18–552 Author chain Q； PDBConstruct 1–535； UniProt 18–552

Lipoprotein

Escherichia coli O127:H6 str. E2348/69

UniProt B7UTD2

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 34	Outer membrane lipoprotein BfpB × 17 （Q47068）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	B7UTD2_ECO27
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain R； PDBConstruct 1–114； UniProt 20–133 Author chain S； PDBConstruct 1–114； UniProt 20–133 Author chain T； PDBConstruct 1–114； UniProt 20–133 Author chain U； PDBConstruct 1–114； UniProt 20–133 Author chain V； PDBConstruct 1–114； UniProt 20–133 Author chain W； PDBConstruct 1–114； UniProt 20–133 Author chain X； PDBConstruct 1–114； UniProt 20–133 Author chain Y； PDBConstruct 1–114； UniProt 20–133 Author chain Z； PDBConstruct 1–114； UniProt 20–133 Author chain a； PDBConstruct 1–114； UniProt 20–133 Author chain b； PDBConstruct 1–114； UniProt 20–133 Author chain c； PDBConstruct 1–114； UniProt 20–133 Author chain d； PDBConstruct 1–114； UniProt 20–133 Author chain e； PDBConstruct 1–114； UniProt 20–133 Author chain f； PDBConstruct 1–114； UniProt 20–133 Author chain g； PDBConstruct 1–114； UniProt 20–133 Author chain h； PDBConstruct 1–114； UniProt 20–133

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	9u5s
Deposition date deposition_date	2025-03-21
Structure title title	The structure of the BfpBG complex in the T4bP system
Keywords keywords	SECRETIN FAMILY, C17 SYMMETRY, T4bP, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method method	ELECTRON MICROSCOPY

▼

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.

9u5s__assembly_1__model_1

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

Download this curve (.dat)

9u5s__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

9u5s__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	76.85 Å
Rg (electron density)	76.47 Å
Total Rg	76.55 Å
Atom count	71791
Residues	9469
Excluded volume	1272900 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`9u5s__assembly_1__model_1`	34-meric （34）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Outer membrane lipoprotein BfpB
Molecular weight formula_weight	56512.4 kDa
Source method src_method	man
Copy count entity_count	17

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q
Atom count atom_count	71791

CSGNGFYKDNLGVIDKNILHADTSLLKSKNKEHYKSSDMVSKTDSIYIGNSSFQTYHGEPLPGKLEGVHGIILRSSTPLGFDEVLSMIQDSSGIPIVKHTTKDVISGGVSSKSLAATVAEKMNSATGGKSTDQFDHLLLEVSSEHQLMDVNYQGALSTFLDKVAANYNLYWTYESGRIAFSNEETKRFSISILPGGKYTSKNSISSDSNSSSGSSGSSGSSSSDSGAELKFDSDVDFWKDIENSIKLILGSDGSYSISTSTSSVIVRTSSANMKKINEYINTLNAQLERQVTIDVAIYNVTTTDSSDLAMSLEALLKHNGGVLGSVSTSNFAATSGTPSFTGYLNGNGDSSNQVLLNLLAEKGKVSVVTSASVTTMSGQPVPLKVGNDRTYVSEIGTVLSQSSTSTTASTSTVTSGFLMNLLPQVADDGNILLQYGVTLSELVGSNNGFDQATVNGTVIQLPNVDSTTFVQSSMLRNGNTLVLAGYEKKRNESVDQGVGTTSFKLLGGALNGSASRTVTVICITPRIIDLKASGE

Source Source

Source organism organism	Escherichia coli O127:H6 str. E2348/69
NCBI taxonomy ID ncbi_taxonomy_id	574521
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Lipoprotein
Molecular weight formula_weight	12656.1 kDa
Source method src_method	man
Copy count entity_count	17

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	R,S,T,U,V,W,X,Y,Z,a,b,c,d,e,f,g,h

ESANKNEKLFSGDTTSVALQASERTIKNAKADWSVIKGQTLYGVLSDWAQQSGWTVLWHANYNYTLNASAVFKDMSLDDAVKKLLESMGNVSPRVFIKFYNGNHVILVTQSPEG

Source Source

Source organism organism	Escherichia coli O127:H6 str. E2348/69
NCBI taxonomy ID ncbi_taxonomy_id	574521
Host organism host_organism	Escherichia coli

▶

Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	2.560 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	2.56 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	75445

The structure of the BfpBG complex in the T4bP system

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

Outer membrane lipoprotein BfpB

State in the Current Structure

Other States of the Same Protein in the Database

Lipoprotein

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

9u5s__assembly_1__model_1

9u5s__assembly_1__model_1 | I(q)

9u5s__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

7. Citations (1)

The structure of the BfpBG complex in the T4bP system

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

Outer membrane lipoprotein BfpB

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Lipoprotein

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

9u5s__assembly_1__model_1

9u5s__assembly_1__model_1 | I(q)

9u5s__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

7. Citations (1)