SAXSdb — 1cy9

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

DNA TOPOISOMERASE I

Escherichia coli

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 214–477 Chain B； UniProt 214–477	Fragment：30 KDA FRAGMENT COMPRISING DOMAINS II AND III	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6；277 K；11-13%(W/V) PEG 3500, 20MM MES PH 6.0, 50MM KCL, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.80 Å R-free 0.242

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1CY9	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CY0 COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH 3'-5'-ADENOSINE DIPHOSPHATE Deposited 1999-08-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–597（597 aa） Fragment：67 KDA N-TERMINAL FRAGMENT OF E.COLI TOPOISOMERASE I	Not recorded	A3P ADENOSINE-3'-5'-DIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions MICRODIALYSIS；pH 5；287 K；2.14M ammonium sulfate, pH 5.0, MICRODIALYSIS, temperature 287K	Resolution 2.45 Å R-free 0.274
1CY1 COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH 5'PTPTPT Deposited 1999-08-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–597（597 aa） Fragment：67 KDA N-TERMINAL FRAGMENT OF E.COLI TOPOISOMERASE I	Not recorded	PO4 PHOSPHATE ION × 1 TMP THYMIDINE-5'-PHOSPHATE × 2 THP THYMIDINE-3',5'-DIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；287 K；2.3M ammonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 287K	Resolution 2.30 Å R-free 0.307
1CY2 COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH TPTPTP3' Deposited 1999-08-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–597（597 aa） Fragment：67 KDA N-TERMINAL FRAGMENT OF E.COLI TOPOISOMERASE I	Not recorded	PO4 PHOSPHATE ION × 1 TMP THYMIDINE-5'-PHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；287 K；2.3M ammonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 287K	Resolution 2.30 Å R-free 0.284
1CY4 COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH 5'pTpTpTp3' Deposited 1999-08-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–597（597 aa） Fragment：67 KDA N-TERMINAL FRAGMENT OF E.COLI TOPOISOMERASE I	Not recorded	PO4 PHOSPHATE ION × 3 TMP THYMIDINE-5'-PHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；2.2M AMMONIUM SULFATE, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.55 Å R-free 0.299
1CY6 COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH 3' THYMIDINE MONOPHOSPHATE Deposited 1999-08-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–597（597 aa） Fragment：67 KDA N-TERMINAL FRAGMENT OF E.COLI TOPOISOMERASE I	Not recorded	PO4 PHOSPHATE ION × 3 T3P THYMIDINE-3'-PHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；287 K；2.2M AMMONIUM SULFATE, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 287K	Resolution 2.50 Å R-free 0.309
1CY7 COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH 5'-THYMIDINE MONOPHOSPHATE Deposited 1999-08-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–597（597 aa） Fragment：67 KDA N-TERMINAL FRAGMENT OF E.COLI TOPOISOMERASE I	Mutation：GLY-SER ATTACHED AT N-TERMINUS DUE TO CONSTRUCT	PO4 PHOSPHATE ION × 1 TMP THYMIDINE-5'-PHOSPHATE × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；2.3M AMMONIUM SULFATE, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.40 Å R-free 0.295
1CY8 COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH 5'-THYMIDINE MONOPHOSPHATE AND 3'-THYMIDINE MONOPHOSPHATE Deposited 1999-08-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–597（597 aa） Fragment：67 KDA N-TERMINAL FRAGMENT OF E.COLI TOPOISOMERASE I	Not recorded	PO4 PHOSPHATE ION × 1 T3P THYMIDINE-3'-PHOSPHATE × 1 TMP THYMIDINE-5'-PHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；287 K；2.2M AMMONIUM SULFATE, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 287K	Resolution 2.45 Å R-free 0.295
1CYY CRYSTAL STRUCTURE OF THE 30 KDA FRAGMENT OF E. COLI DNA TOPOISOMERASE I. HEXAGONAL FORM Deposited 1999-08-31	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 214–477（264 aa） Fragment：30 KDA FRAGMENT COMPRISING DOMAINS II AND III Chain B 214–477（264 aa） Fragment：30 KDA FRAGMENT COMPRISING DOMAINS II AND III	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；296 K；2M AMMONIUM SULFATE, 100MM HEPES PH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 2.15 Å R-free 0.282
1CYY CRYSTAL STRUCTURE OF THE 30 KDA FRAGMENT OF E. COLI DNA TOPOISOMERASE I. HEXAGONAL FORM Deposited 1999-08-31	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 214–477（264 aa） Fragment：30 KDA FRAGMENT COMPRISING DOMAINS II AND III Chain B 214–477（264 aa） Fragment：30 KDA FRAGMENT COMPRISING DOMAINS II AND III	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；296 K；2M AMMONIUM SULFATE, 100MM HEPES PH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 2.15 Å R-free 0.282
1CYY CRYSTAL STRUCTURE OF THE 30 KDA FRAGMENT OF E. COLI DNA TOPOISOMERASE I. HEXAGONAL FORM Deposited 1999-08-31	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 214–477（264 aa） Fragment：30 KDA FRAGMENT COMPRISING DOMAINS II AND III Chain B 214–477（264 aa） Fragment：30 KDA FRAGMENT COMPRISING DOMAINS II AND III	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；296 K；2M AMMONIUM SULFATE, 100MM HEPES PH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 2.15 Å R-free 0.282
1ECL AMINO TERMINAL 67KDA DOMAIN OF ESCHERICHIA COLI DNA TOPOISOMERASE I (RESIDUES 2-590 OF MATURE PROTEIN) CLONING ARTIFACT ADDS TWO RESIDUES TO THE AMINO-TERMINUS WHICH WERE NOT OBSERVED IN THE EXPERIMENTAL ELECTRON DENSITY (GLY-2, SER-1). Deposited 1995-05-05	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–597（597 aa）	Mutation：GLY SER INSERTION AT N-TERMINUS, INSERTION OF STOP CODON AT 598; ENGINEERED	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.90 Å
1MW8 Crystal Structure of a Complex between H365R mutant of 67 kDA N-terminal fragment of E. coli DNA Topoisomerase I and 5'-ACTTCGGGATG-3' Deposited 2002-09-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: dimeric	Chain X 1–592（592 aa） Fragment：67 kDa N-terminal fragment	Mutation：H365R	SO4 SULFATE ION × 5 TMP THYMIDINE-5'-PHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；287 K；ammonium sulfate, sodium acetate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 287K	Resolution 1.90 Å R-free 0.273
1MW9 Crystal Structure of H365R mutant of 67 kDA N-terminal fragment of E. coli DNA Topoisomerase I Deposited 2002-09-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain X 1–592（592 aa） Fragment：67 kDa N-terminal fragment	Mutation：H365R	SO4 SULFATE ION × 9	X-RAY DIFFRACTION X-ray crystallization conditions DIALYSIS；pH 8；287 K；ammonium sulfate, pH 8, DIALYSIS, temperature 287K	Resolution 1.67 Å R-free 0.216
1YUA C-TERMINAL DOMAIN OF ESCHERICHIA COLI TOPOISOMERASE I Deposited 1995-03-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 745–865（121 aa） Fragment：122 C-TERMINAL RESIDUES	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
3PWT Crystal structure of mutant E.coli topoisomerase IA Deposited 2010-12-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–596（596 aa） Fragment：N-terminal catalytical domain, 67K	Mutation：D111N	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.4；288 K；2M ammonium sulfate, pH 7.4, VAPOR DIFFUSION, temperature 288K	Resolution 1.90 Å R-free 0.249
9GDA RNAP-TopoI complex on duplex scaffold Deposited 2024-08-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: nonameric	Chain F 1–865（865 aa）	Not recorded	MG MAGNESIUM ION × 1 ZN ZINC ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.70 Å
9GDB RNAP-TopoI complex on bubble scaffold - consensus reconstruction Deposited 2024-08-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: nonameric	Chain F 1–865（865 aa）	Not recorded	MG MAGNESIUM ION × 1 ZN ZINC ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
9GDC RNAP-TopoI complex on bubble scaffold - single-bubble configuration Deposited 2024-08-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: nonameric	Chain F 1–865（865 aa）	Not recorded	MG MAGNESIUM ION × 1 ZN ZINC ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.30 Å
9GDD RNAP-TopoI complex on bubble scaffold - two-bubble configuration Deposited 2024-08-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: nonameric	Chain F 1–865（865 aa）	Not recorded	MG MAGNESIUM ION × 1 ZN ZINC ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.30 Å
9GDE RNAP-TopoI complex on long-overhang scaffold - orientation 1 Deposited 2024-08-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: nonameric	Chain F 1–865（865 aa）	Not recorded	MG MAGNESIUM ION × 1 ZN ZINC ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.00 Å
9GDH RNAP-TopoI complex on long-overhang scaffold - orientation 2 Deposited 2024-08-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: nonameric	Chain F 1–865（865 aa）	Not recorded	MG MAGNESIUM ION × 1 ZN ZINC ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å

19 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TOP1_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–264； UniProt 214–477 Author chain B； PDBConstruct 1–264； UniProt 214–477

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	1cy9
Deposition date deposition_date	1999-08-31
Structure title title	CRYSTAL STRUCTURE OF THE 30 KDA FRAGMENT OF E. COLI DNA TOPOISOMERASE I. MONOCLINIC FORM
Keywords keywords	DNA TOPOISOMERASE, DECATENATING ENZYME, ISOMERASE; ISOMERASE
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	36.56 Å
Radius of gyration Rg (electron density) rg_electron	36.99 Å
Forward intensity I(0) i0	48690000.00
Molecular weight molecular_weight	54718.0 kDa
Excluded volume excluded_volume	68382 Å³
Envelope volume envelope_volume	103620 Å³
Hydration-shell volume shell_volume	26708 Å³
Envelope diameter envelope_diameter	121.9 Å
Shell Rg shell_rg	37.36 Å
Envelope Rg envelope_rg	36.42 Å
Shape Rg shape_rg	37.03 Å
Total Rg total_rg	36.90 Å
Total atoms total_atoms	3846
Residues n_residues	488
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	115.1 Å
Rg (real space) rg_real	37.02 Å
Rg uncertainty (real space) rg_real_error	1.33 Å
I(0) (real space) i0_real	4.8690e+07
I(0) uncertainty (real space) i0_real_error	8.7820e+05
Rg (reciprocal space) rg_reciprocal	36.74 Å
I(0) (reciprocal space) i0_reciprocal	48680000.0000
Solution quality estimate total_estimate	0.7623
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	45.5 Å
Skewness Skewness skewness	0.482
Kurtosis Kurtosis kurtosis	-0.520
Angular range angular_range	— – 0.2150 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2185000.0000
Real-space data points n_real_points	44
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.774; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.580; Smooth: 0.006

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1cy9a_
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	d1cy9b_
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 (4 domains)

Domain ID domain_id	1cy9A01
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	1cy9A02
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	20 — Topoisomerase I; domain 3
Homologous superfamily homologous superfamily	10 — Topoisomerase I, domain 3

Domain ID domain_id	1cy9B01
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	1cy9B02
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	20 — Topoisomerase I; domain 3
Homologous superfamily homologous superfamily	10 — Topoisomerase I, domain 3

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8. Citations (1)

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Unit-cell length a length_a	36.820 Å
Unit-cell length b length_b	146.550 Å
Unit-cell length c length_c	64.570 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	106.48 °
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	1.800 Å
Low-resolution limit resolution_low	27.500 Å
R factor r_factor	0.2050
R_work r_work	0.2050
R_free r_free	0.2420

Description description	DNA TOPOISOMERASE I
Molecular weight formula_weight	29659.6 kDa
EC 编号 ec_number	5.99.1.2
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	4355

CRYSTAL STRUCTURE OF THE 30 KDA FRAGMENT OF E. COLI DNA TOPOISOMERASE I. MONOCLINIC FORM

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

DNA TOPOISOMERASE I

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	83333
宿主生物 host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	509

fit	/app/data/saxs_computation/cy/1cy9/1cy9.fit
pddf	/app/data/pr_computation/cy/1cy9/1cy9.pr.out
profile	/app/data/saxs_computation/cy/1cy9/1cy9.dat