SAXSdb — 2oo6

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

Putative L-alanine-DL-glutamate epimerase

Burkholderia xenovorans

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 8	SULFATE ION × 16 water × 8	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q13PB7_BURXL
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–401； UniProt 2–399

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	2oo6
Deposition date deposition_date	2007-01-25
Structure title title	Crystal structure of putative L-alanine-DL-glutamate epimerase from Burkholderia xenovorans strain LB400
Keywords keywords	;STRUCTURAL GENOMICS, ENOLASE, PSI-2, Protein Structure Initiative, New York SGX Research Center for Structural Genomics, NYSGXRC, ISOMERASE ;; ISOMERASE
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.

2oo6__assembly_1__model_1

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

Download this curve (.dat)

2oo6__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2oo6__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	41.69 Å
Rg (electron density)	40.72 Å
Total Rg	41.27 Å
Atom count	24904
Residues	3144
Excluded volume	441270 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2oo6__assembly_1__model_1`	octameric （8）	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	Putative L-alanine-DL-glutamate epimerase
Molecular weight formula_weight	45960.0 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	3500

MSLKVVSVDTLCCDAGWRNYHFVKLTTDEGIVGWSEFDEGFGSPGVTAVIEQLGKRLVGASVMEHERFFAEAYCLTRPATGGVVSEGIGAIENALLDAKAKTLNVPCYELLGGKLRDRVPVYWSHCPTWRINHPKFFGPPVTDLDGVKRTAEEARERQFRAIKTNIFIHDDGPLHAWRPGFAVPFQPALNVDRKVLRNLRAHLEALRDGAGPDVEILLDLNFNAKPEGYLKILRELADFDLFWVEIDSYSPQGLAYVRNHSPHPISSCETLFGIREFKPFFDANAVDVAIVDTIWNGVWQSMKIAAFADAHDINVAPHNFYGHLCTMINANFAAAVPNLRIMETDIDRLAWEDELFTHAPEYQNGELIIPDRPGWGTDPVEEAILAHPPKVMGGLLQYKRSEGHHHHHH

Source Source

Source organism organism	Burkholderia xenovorans
NCBI taxonomy ID ncbi_taxonomy_id	266265
Host organism host_organism	Escherichia coli BL21(DE3)

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 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	323

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6. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id	2oo6A01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily	10 — Enolase-like, N-terminal domain

Domain ID domain_id	2oo6A02
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	120 — Enolase-like C-terminal domain

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Unit-cell length a length_a	104.906 Å
Unit-cell length b length_b	104.906 Å
Unit-cell length c length_c	145.658 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	16

Space group space_group	I 4 2 2
Space-group number int_tables_number	97
Crystal system crystal_system	—

Resolution resolution	1.800 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.1570
R_work r_work	0.1560
R_free r_free	0.1920

Crystal structure of putative L-alanine-DL-glutamate epimerase from Burkholderia xenovorans strain LB400

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

Putative L-alanine-DL-glutamate epimerase

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

2oo6__assembly_1__model_1

2oo6__assembly_1__model_1 | I(q)

2oo6__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

CATH v4.4 (2 domains)

7. Citations (1)

Crystal structure of putative L-alanine-DL-glutamate epimerase from Burkholderia xenovorans strain LB400

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

Putative L-alanine-DL-glutamate epimerase

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

2oo6__assembly_1__model_1

2oo6__assembly_1__model_1 | I(q)

2oo6__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

CATH v4.4 (2 domains)

7. Citations (1)