SAXSdb — 1ecm

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

ENDO-OXABICYCLIC TRANSITION STATE ANALOGUE

Escherichia coli

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC ACID × 4 water × 4	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC ACID × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PHEA_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–109； UniProt 1–109 Author chain B； PDBConstruct 1–109； UniProt 1–109

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	1ecm
Deposition date deposition_date	1994-11-28
Structure title title	ATOMIC STRUCTURE OF THE BURIED CATALYTIC POCKET OF ESCHERICHIA COLI CHORISMATE MUTASE
Keywords keywords	P-PROTEIN, CHORISMATE MUTASE DOMAIN, CHORISMATE MUTASE; CHORISMATE MUTASE
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.

1ecm__assembly_1__model_1

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

Download this curve (.dat)

1ecm__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1ecm__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	34.43 Å
Rg (electron density)	35.04 Å
Total Rg	35.03 Å
Atom count	3130
Residues	372
Excluded volume	55713 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1ecm__assembly_1__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1ecm__assembly_2__model_1`	dimeric （2）	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	ENDO-OXABICYCLIC TRANSITION STATE ANALOGUE
Molecular weight formula_weight	12549.7 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	1642

MTSENPLLALREKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLIIEDSVLTQQALLQQHLNKINPHSARIAFL

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562

Entity 2 Entity 2 non-polymer

Description description	8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC ACID
Molecular weight formula_weight	228.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	77

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1ecma_
Class class	a — All alpha proteins
Fold Fold fold	a.130 — Chorismate mutase II
Superfamily Superfamily superfamily	a.130.1 — Chorismate mutase II
Family Family family	a.130.1.1 — Dimeric chorismate mutase

Domain ID domain_id	d1ecmb_
Class class	a — All alpha proteins
Fold Fold fold	a.130 — Chorismate mutase II
Superfamily Superfamily superfamily	a.130.1 — Chorismate mutase II
Family Family family	a.130.1.1 — Dimeric chorismate mutase

CATH v4.4 (2 domains)

Domain ID domain_id	1ecmA00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	59 — Chorismate Mutase Domain, subunit A
Homologous superfamily homologous superfamily	10 — Chorismate mutase

Domain ID domain_id	1ecmB00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	59 — Chorismate Mutase Domain, subunit A
Homologous superfamily homologous superfamily	10 — Chorismate mutase

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Unit-cell length a length_a	80.830 Å
Unit-cell length b length_b	80.830 Å
Unit-cell length c length_c	83.320 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	P 32 2 1
Space-group number int_tables_number	154
Crystal system crystal_system	—

Resolution resolution	2.200 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.1920
R_work r_work	0.1920
R_free r_free	0.2310

ATOMIC STRUCTURE OF THE BURIED CATALYTIC POCKET OF ESCHERICHIA COLI CHORISMATE MUTASE

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

ENDO-OXABICYCLIC TRANSITION STATE ANALOGUE

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

1ecm__assembly_1__model_1

1ecm__assembly_1__model_1 | I(q)

1ecm__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

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) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

ATOMIC STRUCTURE OF THE BURIED CATALYTIC POCKET OF ESCHERICHIA COLI CHORISMATE MUTASE

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

ENDO-OXABICYCLIC TRANSITION STATE ANALOGUE

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

1ecm__assembly_1__model_1

1ecm__assembly_1__model_1 | I(q)

1ecm__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

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) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)