SAXSdb — 3n0c

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

Thymidylate synthase thyX

Thermotoga maritima

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	;2'-DEOXYURIDINE 5'-MONOPHOSPHATE ; × 4 FLAVIN-ADENINE DINUCLEOTIDE × 4 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	THYX_THEMA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 13–232； UniProt 1–220 Author chain B； PDBConstruct 13–232； UniProt 1–220 Author chain C； PDBConstruct 13–232； UniProt 1–220 Author chain D； PDBConstruct 13–232； UniProt 1–220

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	3n0c
Deposition date deposition_date	2010-05-13
Structure title title	TM0449 mutant crystal grown by hanging drop method
Keywords keywords	Crystals in loops, thyX, FDTS, TRANSFERASE; TRANSFERASE
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.

3n0c__assembly_1__model_1

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

Download this curve (.dat)

3n0c__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3n0c__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	28.86 Å
Rg (electron density)	28.47 Å
Total Rg	29.25 Å
Atom count	7425
Residues	862
Excluded volume	132190 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3n0c__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 (4)

Entity 1 Entity 1 polymer

Description description	Thymidylate synthase thyX
Molecular weight formula_weight	27312.5 kDa
EC 编号 ec_number	2.1.1.148
Mutation mutation	F158A,W160A
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	7471

MGSDKIHHHHHHMKIDILDKGFVELVDVMGNDLSAVRAARVSFDMGLKDEERDRHLIEYLMKHGHETPFEHIVFTFHVKAPIFVARQWFRHRIASYNELSGRYSKLSYEFYIPSPERLEGYKTTIPPERVTEKISEIVDKAYRTYLELIESGVPREVARIVLPLNLYTRAFATVNARSLMNFLNLRADSHAQWEIQQYALAIARIFKEKCPWTFEAFLKYAYKGDILKEVQV

Source Source

Source organism organism	Thermotoga maritima
NCBI taxonomy ID ncbi_taxonomy_id	2336
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	;2'-DEOXYURIDINE 5'-MONOPHOSPHATE ;
Molecular weight formula_weight	308.2 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 3 Entity 3 non-polymer

Description description	FLAVIN-ADENINE DINUCLEOTIDE
Molecular weight formula_weight	785.5 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	46

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6. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (5 domains)

Domain ID domain_id	d3n0ca1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.207 — Thymidylate synthase-complementing protein Thy1
Superfamily Superfamily superfamily	d.207.1 — Thymidylate synthase-complementing protein Thy1
Family Family family	d.207.1.1 — Thymidylate synthase-complementing protein Thy1

Domain ID domain_id	d3n0ca2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d3n0cb_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.207 — Thymidylate synthase-complementing protein Thy1
Superfamily Superfamily superfamily	d.207.1 — Thymidylate synthase-complementing protein Thy1
Family Family family	d.207.1.1 — Thymidylate synthase-complementing protein Thy1

Domain ID domain_id	d3n0cc_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.207 — Thymidylate synthase-complementing protein Thy1
Superfamily Superfamily superfamily	d.207.1 — Thymidylate synthase-complementing protein Thy1
Family Family family	d.207.1.1 — Thymidylate synthase-complementing protein Thy1

Domain ID domain_id	d3n0cd_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.207 — Thymidylate synthase-complementing protein Thy1
Superfamily Superfamily superfamily	d.207.1 — Thymidylate synthase-complementing protein Thy1
Family Family family	d.207.1.1 — Thymidylate synthase-complementing protein Thy1

CATH v4.4 (4 domains)

Domain ID domain_id	3n0cA00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily	170 —

Domain ID domain_id	3n0cB00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily	170 —

Domain ID domain_id	3n0cC00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily	170 —

Domain ID domain_id	3n0cD00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily	170 —

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Unit-cell length a length_a	54.549 Å
Unit-cell length b length_b	116.718 Å
Unit-cell length c length_c	141.202 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	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.1958
R_work r_work	0.1931
R_free r_free	0.2475

TM0449 mutant crystal grown by hanging drop method

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

Thymidylate synthase thyX

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

3n0c__assembly_1__model_1

3n0c__assembly_1__model_1 | I(q)

3n0c__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) 9 domains

SCOP 2.08 (5 domains)

CATH v4.4 (4 domains)

7. Citations (2)

TM0449 mutant crystal grown by hanging drop method

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

Thymidylate synthase thyX

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

3n0c__assembly_1__model_1

3n0c__assembly_1__model_1 | I(q)

3n0c__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) 9 domains

SCOP 2.08 (5 domains)

CATH v4.4 (4 domains)

7. Citations (2)