SAXSdb — 1llw

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

Ferredoxin-dependent glutamate synthase

Synechocystis sp. PCC 6803

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	FLAVIN MONONUCLEOTIDE × 1 FE3-S4 CLUSTER × 1 2-OXOGLUTARIC ACID × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	GLTS_SYNY3
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–1520； UniProt 37–1556

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	1llw
Deposition date deposition_date	2002-04-30
Structure title title	Structural studies on the synchronization of catalytic centers in glutamate synthase: complex with 2-oxoglutarate
Keywords keywords	Ntn amidotransferase, glutamate synthase, chanelling, Oxidoreductase; OXIDOREDUCTASE
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.

1llw__assembly_1__model_1

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

Download this curve (.dat)

1llw__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1llw__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	33.33 Å
Rg (electron density)	32.41 Å
Total Rg	33.02 Å
Atom count	11359
Residues	1475
Excluded volume	201940 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1llw__assembly_1__model_1`	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 (5)

Entity 1 Entity 1 polymer

Description description	Ferredoxin-dependent glutamate synthase
Molecular weight formula_weight	165711.7 kDa
EC 编号 ec_number	1.4.7.1
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	11408

CGVGFIANLRGKPDHTLVEQALKALGCMEHRGGCSADNDSGDGAGVMTAIPRELLAQWFNTRNLPMPDGDRLGVGMVFLPQEPSAREVARAYVEEVVRLEKLTVLGWREVPVNSDVLGIQAKNNQPHIEQILVTCPEGCAGDELDRRLYIARSIIGKKLAEDFYVCSFSCRTIVYKGMVRSIILGEFYLDLKNPGYTSNFAVYHRRFSTNTMPKWPLAQPMRLLGHNGEINTLLGNINWMAAREKELEVSGWTKAELEALTPIVNQANSDSYNLDSALELLVRTGRSPLEAAMILVPEAYKNQPALKDYPEISDFHDYYSGLQEPWDGPALLVFSDGKIVGAGLDRNGLRPARYCITKDDYIVLGSEAGVVDLPEVDIVEKGRLAPGQMIAVDLAEQKILKNYQIKQQAAQKYPYGEWIKIQRQTVASDSFAEKTLFNDAQTVLQQQAAFGYTAEDVEMVVVPMASQGKEPTFCMGDDTPLAVLSHKPRLLYDYFKQRFAQVTNPPIDPLRENLVMSLAMFLGKRGNLLEPKAESARTIKLRSPLVNEVELQAIKTGQLQVAEVSTLYDLDGVNSLEDALTNLVKTAIATVQAGAEILVLTDRPNGAILTENQSFIPPLLAVGAVHHHLIRAGLRLKASLIVDTAQCWSTHHFACLVGYGASAICPYLALESVRQWWLDEKTQKLMENGRLDRIDLPTALKNYRQSVEAGLFKILSKMGISLLASYHGAQIFEAIGLGAELVEYAFAGTTSRVGGLTIADVAGEVMVFHGMAFPEMAKKLENFGFVNYRPGGEYHMNSPEMSKSLHKAVAAYKVGGNGNNGEAYDHYELYRQYLKDRPVTALRDLLDFNADQPAISLEEVESVESIVKRFCTGGMSLGALSREAHETLAIAMNRLGAKSNSGEGGEDVVRYLTLDDVDSEGNSPTLPHLHGLQNGDTANSAIKQIASGRFGVTPEYLMSGKQLEIKMAQGAKPGEGGQLPGKKVSEYIAMLRRSKPGVTLISPPPHHDIYSIEDLAQLIYDLHQINPEAQVSVKLVAEIGIGTIAAGVAKANADIIQISGHDGGTGASPLSSIKHAGSPWELGVTEVHRVLMENQLRDRVLLRADGGLKTGWDVVMAALMGAEEYGFGSIAMIAEGCIMARVCHTNNCPVGVATQQERLRQRFKGVPGQVVNFFYFIAEEVRSLLAHLGYRSLDDIIGRTDLLKVRSDVQLSKTQNLTLDCLLNLPDTKQNRQWLNHEPVHSNGPVLDDDILADPDIQEAINHQTTATKTYRLVNTDRTVGTRLSGAIAKKYGNNGFEGNITLNFQGAAGQSFGAFNLDGMTLHLQGEANDYVGKGMNGGEIVIVPHPQASFAPEDNVIIGNTCLYGATGGNLYANGRAGERFAVRNSVGKAVIEGAGDHCCEYMTGGVIVVLGPVGRNVGAGMTGGLAYFLDEVGDLPEKINPEIITLQRITASKGEEQLKSLITAHVEHTGSPKGKAILANWSDYLGKFWQAVPPSEKDSPEANNDVSLTGEKTLTSV

Source Source

Source organism organism	Synechocystis sp. PCC 6803
NCBI taxonomy ID ncbi_taxonomy_id	1148
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	FLAVIN MONONUCLEOTIDE
Molecular weight formula_weight	456.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	FE3-S4 CLUSTER
Molecular weight formula_weight	295.8 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	2-OXOGLUTARIC ACID
Molecular weight formula_weight	146.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	49

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6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1llwa1
Class class	b — All beta proteins
Fold Fold fold	b.80 — Single-stranded right-handed beta-helix
Superfamily Superfamily superfamily	b.80.4 — Alpha subunit of glutamate synthase, C-terminal domain
Family Family family	b.80.4.1 — Alpha subunit of glutamate synthase, C-terminal domain

Domain ID domain_id	d1llwa2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.4 — FMN-linked oxidoreductases
Family Family family	c.1.4.1 — FMN-linked oxidoreductases

Domain ID domain_id	d1llwa3
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.1 — Class II glutamine amidotransferases

CATH v4.4 (4 domains)

Domain ID domain_id	1llwA01
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	1llwA02
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	70 — Aldolase class I

Domain ID domain_id	1llwA03
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	70 — Aldolase class I

Domain ID domain_id	1llwA04
Class class	2 — Mainly Beta
Architecture architecture	160 — 3 Solenoid
Topology topology	20 — Pectate Lyase C-like
Homologous superfamily homologous superfamily	60 — Glutamate synthase, alpha subunit, C-terminal domain

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Unit-cell length a length_a	166.521 Å
Unit-cell length b length_b	166.521 Å
Unit-cell length c length_c	219.874 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	8

Space group space_group	P 43 21 2
Space-group number int_tables_number	96
Crystal system crystal_system	—

Resolution resolution	2.700 Å
Low-resolution limit resolution_low	12.000 Å
R factor r_factor	0.2359
R_work r_work	0.2345
R_free r_free	0.2927

Structural studies on the synchronization of catalytic centers in glutamate synthase: complex with 2-oxoglutarate

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

Ferredoxin-dependent glutamate synthase

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

1llw__assembly_1__model_1

1llw__assembly_1__model_1 | I(q)

1llw__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) 7 domains

SCOP 2.08 (3 domains)

CATH v4.4 (4 domains)

7. Citations (1)

Structural studies on the synchronization of catalytic centers in glutamate synthase: complex with 2-oxoglutarate

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

Ferredoxin-dependent glutamate synthase

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

1llw__assembly_1__model_1

1llw__assembly_1__model_1 | I(q)

1llw__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) 7 domains

SCOP 2.08 (3 domains)

CATH v4.4 (4 domains)

7. Citations (1)