2m6k

Solution structure of the Escherichia coli apo ferric enterobactin binding protein

Method: SOLUTION NMR

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

Ferrienterobactin-binding periplasmic protein

Escherichia coli

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FEPB_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 24–315； UniProt 27–318

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	2m6k
Deposition date deposition_date	2013-04-05
Structure title title	Solution structure of the Escherichia coli apo ferric enterobactin binding protein
Keywords keywords	periplasmic, siderophore, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method method	SOLUTION NMR

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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.

2m6k__assembly_1__model_23

Assembly 1 · Model 23 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2m6k__assembly_1__model_23 | I(q)

100 plotted points; both axes use logarithmic scales.

2m6k__assembly_1__model_23 | P(r) · Pending

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

Rg（Guinier）	21.24 Å
Rg (electron density)	20.17 Å
Total Rg	21.11 Å
Atom count	4462
Residues	292
Excluded volume	39603 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2m6k__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	2	`2m6k__assembly_1__model_2`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	3	`2m6k__assembly_1__model_3`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	4	`2m6k__assembly_1__model_4`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	5	`2m6k__assembly_1__model_5`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	6	`2m6k__assembly_1__model_6`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	7	`2m6k__assembly_1__model_7`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	8	`2m6k__assembly_1__model_8`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	9	`2m6k__assembly_1__model_9`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	10	`2m6k__assembly_1__model_10`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	11	`2m6k__assembly_1__model_11`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	12	`2m6k__assembly_1__model_12`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	13	`2m6k__assembly_1__model_13`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	14	`2m6k__assembly_1__model_14`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	15	`2m6k__assembly_1__model_15`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	16	`2m6k__assembly_1__model_16`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	17	`2m6k__assembly_1__model_17`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	18	`2m6k__assembly_1__model_18`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	19	`2m6k__assembly_1__model_19`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	20	`2m6k__assembly_1__model_20`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	21	`2m6k__assembly_1__model_21`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	22	`2m6k__assembly_1__model_22`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	23	`2m6k__assembly_1__model_23`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	24	`2m6k__assembly_1__model_24`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	25	`2m6k__assembly_1__model_25`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	26	`2m6k__assembly_1__model_26`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	27	`2m6k__assembly_1__model_27`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	28	`2m6k__assembly_1__model_28`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	29	`2m6k__assembly_1__model_29`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
1	30	`2m6k__assembly_1__model_30`	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 (1)

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6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d2m6ka_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.92 — Chelatase-like
Superfamily Superfamily superfamily	c.92.2 — 'Helical backbone' metal receptor
Family Family family	c.92.2.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id	2m6kA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1980 — Nitrogenase molybdenum iron protein domain

Domain ID domain_id	2m6kA02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1980 — Nitrogenase molybdenum iron protein domain

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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	1

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

Description description	Ferrienterobactin-binding periplasmic protein
Molecular weight formula_weight	34370.5 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	133860

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	83333
Host organism host_organism	Escherichia coli

Solution structure of the Escherichia coli apo ferric enterobactin binding protein

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

Ferrienterobactin-binding periplasmic protein

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

2m6k__assembly_1__model_23

2m6k__assembly_1__model_23 | I(q)

2m6k__assembly_1__model_23 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

5. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

CATH v4.4 (2 domains)

7. Citations (1)

Solution structure of the Escherichia coli apo ferric enterobactin binding protein

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

Ferrienterobactin-binding periplasmic protein

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

2m6k__assembly_1__model_23

2m6k__assembly_1__model_23 | I(q)

2m6k__assembly_1__model_23 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

5. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

CATH v4.4 (2 domains)

7. Citations (1)