SAXSdb — 1t8z

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

Major outer membrane lipoprotein

Escherichia coli

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 5	SULFATE ION × 2 DODECAETHYLENE GLYCOL × 1 water × 5	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	LPP_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–53； UniProt 22–74 Author chain B； PDBConstruct 1–53； UniProt 22–74 Author chain C； PDBConstruct 1–53； UniProt 22–74 Author chain D； PDBConstruct 1–53； UniProt 22–74 Author chain E； PDBConstruct 1–53； UniProt 22–74

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	1t8z
Deposition date deposition_date	2004-05-13
Structure title title	Atomic Structure of A Novel Tryptophan-Zipper Pentamer
Keywords keywords	LIPOPROTEIN, PROTEIN FOLDING, COILED COIL, PENTAMER, TRYPTOPHAN-ZIPPER, MEMBRANE PROTEIN; MEMBRANE PROTEIN
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.

1t8z__assembly_1__model_1

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

Download this curve (.dat)

1t8z__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1t8z__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	23.72 Å
Rg (electron density)	23.07 Å
Total Rg	24.01 Å
Atom count	2389
Residues	247
Excluded volume	40271 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1t8z__assembly_1__model_1`	pentameric （5）	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 (4)

Entity 1 Entity 1 polymer

Description description	Major outer membrane lipoprotein
Molecular weight formula_weight	6881.2 kDa
Mutation mutation	I6W, L9W, V13W, L16W, V20W, L23W, V27W, M30W, V34W, A37W, A41W, A44W, L48W, M51W
Source method src_method	man
Copy count entity_count	5

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E
Atom count atom_count	2572

SSNAKWDQWSSDWQTWNAKWDQWSNDWNAWRSDWQAWKDDWARWNQRWDNWAT

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	DODECAETHYLENE GLYCOL
Molecular weight formula_weight	546.6 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	183

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6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (5 domains)

Domain ID domain_id	d1t8za_
Class class	h — Coiled coil proteins
Fold Fold fold	h.1 — Parallel coiled-coil
Superfamily Superfamily superfamily	h.1.16 — Outer membrane lipoprotein
Family Family family	h.1.16.1 — Outer membrane lipoprotein

Domain ID domain_id	d1t8zb_
Class class	h — Coiled coil proteins
Fold Fold fold	h.1 — Parallel coiled-coil
Superfamily Superfamily superfamily	h.1.16 — Outer membrane lipoprotein
Family Family family	h.1.16.1 — Outer membrane lipoprotein

Domain ID domain_id	d1t8zc_
Class class	h — Coiled coil proteins
Fold Fold fold	h.1 — Parallel coiled-coil
Superfamily Superfamily superfamily	h.1.16 — Outer membrane lipoprotein
Family Family family	h.1.16.1 — Outer membrane lipoprotein

Domain ID domain_id	d1t8zd_
Class class	h — Coiled coil proteins
Fold Fold fold	h.1 — Parallel coiled-coil
Superfamily Superfamily superfamily	h.1.16 — Outer membrane lipoprotein
Family Family family	h.1.16.1 — Outer membrane lipoprotein

Domain ID domain_id	d1t8ze_
Class class	h — Coiled coil proteins
Fold Fold fold	h.1 — Parallel coiled-coil
Superfamily Superfamily superfamily	h.1.16 — Outer membrane lipoprotein
Family Family family	h.1.16.1 — Outer membrane lipoprotein

CATH v4.4 (5 domains)

Domain ID domain_id	1t8zA00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	190 —

Domain ID domain_id	1t8zB00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	190 —

Domain ID domain_id	1t8zC00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	190 —

Domain ID domain_id	1t8zD00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	190 —

Domain ID domain_id	1t8zE00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	190 —

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Unit-cell length a length_a	30.547 Å
Unit-cell length b length_b	30.665 Å
Unit-cell length c length_c	72.405 Å
Unit-cell angle α angle_alpha	97.37 °
Unit-cell angle β angle_beta	91.94 °
Unit-cell angle γ angle_gamma	113.46 °
Molecules per unit cell Z z_pdb	5

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

Resolution resolution	1.450 Å
Low-resolution limit resolution_low	70.710 Å
R factor r_factor	0.2195
R_work r_work	0.2164
R_free r_free	0.2771

Atomic Structure of A Novel Tryptophan-Zipper Pentamer

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

Major outer membrane 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

1t8z__assembly_1__model_1

1t8z__assembly_1__model_1 | I(q)

1t8z__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (5 domains)

CATH v4.4 (5 domains)

7. Citations (1)

Atomic Structure of A Novel Tryptophan-Zipper Pentamer

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

Major outer membrane 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

1t8z__assembly_1__model_1

1t8z__assembly_1__model_1 | I(q)

1t8z__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (5 domains)

CATH v4.4 (5 domains)

7. Citations (1)