SAXSdb — 2e6c

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

;5'-nucleotidase surE ;

Thermus thermophilus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	MANGANESE (II) ION × 4 SULFATE ION × 9 GLYCEROL × 2 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	SURE_THET8
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–244； UniProt 1–244 Author chain B； PDBConstruct 1–244； UniProt 1–244 Author chain C； PDBConstruct 1–244； UniProt 1–244 Author chain D； PDBConstruct 1–244； UniProt 1–244

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	2e6c
Deposition date deposition_date	2006-12-26
Structure title title	Crystal structure of the stationary phase survival protein SurE from Thermus thermophilus HB8 cocrystallized with manganese and AMP
Keywords keywords	SurE protein, cocrystal structure with manganese ion and AMP, Hydrolase; HYDROLASE
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.

2e6c__assembly_1__model_1

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

Download this curve (.dat)

2e6c__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2e6c__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	29.78 Å
Rg (electron density)	28.94 Å
Total Rg	29.73 Å
Atom count	7437
Residues	952
Excluded volume	132300 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2e6c__assembly_1__model_1`	tetrameric （4）	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 (5)

Entity 1 Entity 1 polymer

Description description	;5'-nucleotidase surE ;
Molecular weight formula_weight	26625.3 kDa
EC 编号 ec_number	3.1.3.5
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	7741

MRILVTNDDGIYSPGLWALAEAASQFGEVFVAAPDTEQSAAGHAITIAHPVRAYPHPSPLHAPHFPAYRVRGTPADCVALGLHLFGPVDLVLSGVNLGSNLGHEIWHSGTVAAAKQGYLFGLSAAAFSVPLNGEVPDFAGLRPWLLRTLETLLRLERPFLVNVNLPLRPKGFLWTRQSVRAYEGVVIPGEDPMGRPFYWFAPRPLKEAEEGTDRWAVAQGFVSATPLRLDLTDETRLQPTLAHD

Source Source

Source organism organism	Thermus thermophilus
NCBI taxonomy ID ncbi_taxonomy_id	300852
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 non-polymer

Description description	MANGANESE (II) ION
Molecular weight formula_weight	54.9 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 3 Entity 3 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	9

Entity 4 Entity 4 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	304

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d2e6ca_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.106 — SurE-like
Superfamily Superfamily superfamily	c.106.1 — SurE-like
Family Family family	c.106.1.0 — automated matches

Domain ID domain_id	d2e6cb_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.106 — SurE-like
Superfamily Superfamily superfamily	c.106.1 — SurE-like
Family Family family	c.106.1.0 — automated matches

Domain ID domain_id	d2e6cc_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.106 — SurE-like
Superfamily Superfamily superfamily	c.106.1 — SurE-like
Family Family family	c.106.1.0 — automated matches

Domain ID domain_id	d2e6cd_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.106 — SurE-like
Superfamily Superfamily superfamily	c.106.1 — SurE-like
Family Family family	c.106.1.0 — automated matches

CATH v4.4 (4 domains)

Domain ID domain_id	2e6cA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1210 — Stationary-phase Survival Protein Sure Homolog; Chain: A,
Homologous superfamily homologous superfamily	10 — Survival protein SurE-like phosphatase/nucleotidase

Domain ID domain_id	2e6cB00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1210 — Stationary-phase Survival Protein Sure Homolog; Chain: A,
Homologous superfamily homologous superfamily	10 — Survival protein SurE-like phosphatase/nucleotidase

Domain ID domain_id	2e6cC00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1210 — Stationary-phase Survival Protein Sure Homolog; Chain: A,
Homologous superfamily homologous superfamily	10 — Survival protein SurE-like phosphatase/nucleotidase

Domain ID domain_id	2e6cD00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1210 — Stationary-phase Survival Protein Sure Homolog; Chain: A,
Homologous superfamily homologous superfamily	10 — Survival protein SurE-like phosphatase/nucleotidase

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Unit-cell length a length_a	132.599 Å
Unit-cell length b length_b	132.599 Å
Unit-cell length c length_c	130.783 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	24

Space group space_group	P 31 2 1
Space-group number int_tables_number	152
Crystal system crystal_system	—

Resolution resolution	2.050 Å
Low-resolution limit resolution_low	46.560 Å
R factor r_factor	0.2080
R_work r_work	0.2080
R_free r_free	0.2490

Crystal structure of the stationary phase survival protein SurE from Thermus thermophilus HB8 cocrystallized with manganese and AMP

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

;5'-nucleotidase surE ;

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

2e6c__assembly_1__model_1

2e6c__assembly_1__model_1 | I(q)

2e6c__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 (5)

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 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)

Crystal structure of the stationary phase survival protein SurE from Thermus thermophilus HB8 cocrystallized with manganese and AMP

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

;5'-nucleotidase surE ;

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

2e6c__assembly_1__model_1

2e6c__assembly_1__model_1 | I(q)

2e6c__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 (5)

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 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)