1gl9

Archaeoglobus fulgidus reverse gyrase complexed with ADPNP

Method: X-RAY DIFFRACTION

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

REVERSE GYRASE

ARCHAEOGLOBUS FULGIDUS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MAGNESIUM ION × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MAGNESIUM ION × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	O29238
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain B； PDBConstruct 1–1054； UniProt 1–1054 Author chain C； PDBConstruct 1–1054； UniProt 1–1054

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	1gl9
Deposition date deposition_date	2001-08-30
Structure title title	Archaeoglobus fulgidus reverse gyrase complexed with ADPNP
Keywords keywords	TOPOISOMERASE, DNA SUPERCOILING, ARCHAEA, HELICASE; TOPOISOMERASE
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.

1gl9__assembly_1__model_1

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

Download this curve (.dat)

1gl9__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1gl9__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	35.62 Å
Rg (electron density)	35.18 Å
Total Rg	35.61 Å
Atom count	8258
Residues	1020
Excluded volume	147590 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1gl9__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1gl9__assembly_2__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 (3)

Entity 1 Entity 1 polymer

Description description	REVERSE GYRASE
Molecular weight formula_weight	121535.0 kDa
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,C
Atom count atom_count	16398

MIPVVYSNLCPVCGGDLESKEIEKHVCFRKKRSLCLFPEDFLLKEFVEFFRKCVGEPRAIQKMWAKRILRKESFAATAPTGVGKTSFGLAMSLFLALKGKRCYVIFPTSLLVIQAAETIRKYAEKAGVGTENLIGYYHGRIPKREKENFMQNLRNFKIVITTTQFLSKHYRELGHFDFIFVDDVDAILKASKNVDKLLHLLGFHYDLKTKSWVGEARGCLMVSTATAKKGKKAELFRQLLNFDIGSSRITVRNVEDVAVNDESISTLSSILEKLGTGGIIYARTGEEAEEIYESLKNKFRIGIVTATKKGDYEKFVEGEIDHLIGTAHYYGTLVRGLDLPERIRFAVFVGCPSFRVTIEDIDSLSPQMVKLLAYLYRNVDEIERLLPAVERHIDEVREILKKVMGKERPQAKDVVVREGEVIFPDLRTYIQGSGRTSRLFAGGLTKGASFLLEDDSELLSAFIERAKLYDIEFKSIDEVDFEKLSRELDESRDRYRRRQEFDLIKPALFIVESPTKARQISRFFGKPSVKVLDGAVVYEIPMQKYVLMVTASIGHVVDLITNRGFHGVLVNGRFVPVYASIKRCRDCGYQFTEDRESCPKCGSENVDNSRSRIEALRKLAHDAEFVIVGTDPDTEGEKIAWDLKNLLSGCGAVKRAEFHEVTRRAILEALESLRDVDENLVKAQVVRRIEDRWIGFVLSQKLWERFNNRNLSAGRAQTLVLGWIIDRFQESRERRKIAIVRDFDLVLEHDEEEFDLTIKLVEEREELRTPLPPYTTETMLSDANRILKFSVKQTMQIAQELFENGLITYHRTDSTRVSDVGQRIAKEYLGDDFVGREWGESGAHECIRPTRPLTRDDVQRLIQEGVLVVEGLRWEHFALYDLIFRRFMASQCRPFKVVVKKYSIEFDGKTAEEERIVRAEGRAYELYRAVWVKNELPTGTFRVKAEVKSVPKVLPFTQSEIIQMMKERGIGRPSTYATIVDRLFMRNYVVEKYGRMIPTKLGIDVFRFLVRRYAKFVSEDRTRDLESRMDAIERGELDYLKALEDMYAEIKSID

Source Source

Source organism organism	ARCHAEOGLOBUS FULGIDUS
NCBI taxonomy ID ncbi_taxonomy_id	224325
Host organism host_organism	ESCHERICHIA COLI BL21(DE3)

Entity 2 Entity 2 non-polymer

Description description	PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
Molecular weight formula_weight	506.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	2

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6. Fold Classification (SCOP + CATH) 22 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d1gl9b1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.16 — Helicase-like domain of reverse gyrase

Domain ID domain_id	d1gl9b2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.16 — Helicase-like domain of reverse gyrase

Domain ID domain_id	d1gl9b3
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.10 — Prokaryotic type I DNA topoisomerase
Superfamily Superfamily superfamily	e.10.1 — Prokaryotic type I DNA topoisomerase
Family Family family	e.10.1.1 — Prokaryotic type I DNA topoisomerase

Domain ID domain_id	d1gl9c1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.16 — Helicase-like domain of reverse gyrase

Domain ID domain_id	d1gl9c2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.16 — Helicase-like domain of reverse gyrase

Domain ID domain_id	d1gl9c3
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.10 — Prokaryotic type I DNA topoisomerase
Superfamily Superfamily superfamily	e.10.1 — Prokaryotic type I DNA topoisomerase
Family Family family	e.10.1.1 — Prokaryotic type I DNA topoisomerase

CATH v4.4 (16 domains)

Domain ID domain_id	1gl9B01
Class class	2 — Mainly Beta
Architecture architecture	20 — Single Sheet
Topology topology	20 — Anthopleurin-A
Homologous superfamily homologous superfamily	30 — reverse gyrase domain

Domain ID domain_id	1gl9B02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	1gl9B03
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	1gl9B04
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	56 — Phenylalanyl-tRNA Synthetase; Chain B, domain 1
Homologous superfamily homologous superfamily	120 —

Domain ID domain_id	1gl9B05
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	140 —

Domain ID domain_id	1gl9B06
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	460 — Topoisomerase I; domain 2
Homologous superfamily homologous superfamily	10 — Topoisomerase I, domain 2

Domain ID domain_id	1gl9B07
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	510 — EV matrix protein fold
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1gl9B08
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	290 — Topoisomerase I; domain 4
Homologous superfamily homologous superfamily	10 — Topoisomerase I, domain 4

Domain ID domain_id	1gl9C01
Class class	2 — Mainly Beta
Architecture architecture	20 — Single Sheet
Topology topology	20 — Anthopleurin-A
Homologous superfamily homologous superfamily	30 — reverse gyrase domain

Domain ID domain_id	1gl9C02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	1gl9C03
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	1gl9C04
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	56 — Phenylalanyl-tRNA Synthetase; Chain B, domain 1
Homologous superfamily homologous superfamily	120 —

Domain ID domain_id	1gl9C05
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	140 —

Domain ID domain_id	1gl9C06
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	460 — Topoisomerase I; domain 2
Homologous superfamily homologous superfamily	10 — Topoisomerase I, domain 2

Domain ID domain_id	1gl9C07
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	510 — EV matrix protein fold
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1gl9C08
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	290 — Topoisomerase I; domain 4
Homologous superfamily homologous superfamily	10 — Topoisomerase I, domain 4

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Unit-cell length a length_a	132.410 Å
Unit-cell length b length_b	68.690 Å
Unit-cell length c length_c	134.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	99.70 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	3.200 Å
Low-resolution limit resolution_low	34.000 Å
R factor r_factor	0.2560
R_work r_work	0.2560
R_free r_free	0.3320

Archaeoglobus fulgidus reverse gyrase complexed with ADPNP

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

REVERSE GYRASE

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

1gl9__assembly_1__model_1

1gl9__assembly_1__model_1 | I(q)

1gl9__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 non-polymer

6. Fold Classification (SCOP + CATH) 22 domains

SCOP 2.08 (6 domains)

CATH v4.4 (16 domains)

7. Citations (1)

Archaeoglobus fulgidus reverse gyrase complexed with ADPNP

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

REVERSE GYRASE

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

1gl9__assembly_1__model_1

1gl9__assembly_1__model_1 | I(q)

1gl9__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 non-polymer

6. Fold Classification (SCOP + CATH) 22 domains

SCOP 2.08 (6 domains)

CATH v4.4 (16 domains)

7. Citations (1)