1qsg

CRYSTAL STRUCTURE OF ENOYL REDUCTASE INHIBITION BY TRICLOSAN

Method: X-RAY DIFFRACTION D_max: 156.3 Å Quality: GOOD

▼

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

ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE

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 × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 1–262 Chain B； UniProt 1–262 Chain C； UniProt 1–262 Chain D； UniProt 1–262	Not recorded	GLC alpha-D-glucopyranose × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 TCL TRICLOSAN × 4	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 4.6；295.15 K；PEG 4000, AMMONIUM ACETATE, SODIUM ACETATE, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 295.15K	Resolution 1.75 Å R-free 0.215
2	Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain E； UniProt 1–262 Chain F； UniProt 1–262 Chain G； UniProt 1–262 Chain H； UniProt 1–262	Not recorded	GLC alpha-D-glucopyranose × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 TCL TRICLOSAN × 4	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 4.6；295.15 K；PEG 4000, AMMONIUM ACETATE, SODIUM ACETATE, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 295.15K	Resolution 1.75 Å R-free 0.215

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 1QSG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1C14 CRYSTAL STRUCTURE OF E COLI ENOYL REDUCTASE-NAD+-TRICLOSAN COMPLEX Deposited 1999-07-20	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–262（262 aa） Chain B 1–262（262 aa）	Not recorded	NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 TCL TRICLOSAN × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；300 K；(NH4)2SO4, PEG400, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 300K	Resolution 2.00 Å R-free 0.263
1D8A E. COLI ENOYL REDUCTASE/NAD+/TRICLOSAN COMPLEX Deposited 1999-10-21	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–262（261 aa） Chain B 2–262（261 aa）	Not recorded	NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 TCL TRICLOSAN × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOUR DIFFUSION；pH 7.5；290 K；PEG 400, NA HEPES, AMMONIUM SULPHATE, pH 7.5, VAPOUR DIFFUSION, temperature 290K	Resolution 2.20 Å R-free 0.294
1DFG X-RAY STRUCTURE OF ESCHERICHIA COLI ENOYL REDUCTASE WITH BOUND NAD AND BENZO-DIAZABORINE Deposited 1997-01-16	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–261（261 aa） Chain B 1–261（261 aa）	Not recorded	NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 NDT 2-(TOLUENE-4-SULFONYL)-2H-BENZO[D][1,2,3]DIAZABORININ-1-OL × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；15% PEG 400, PH5.0 100MM ACETATE, 5MM NAD, 5MM 1,2-DIHYDRO-1-HYDROXY-2- (4-METHYLSULPHONYL)BENZO[E][1,2,3]DIAZABORINE	Resolution 2.50 Å
1DFH X-RAY STRUCTURE OF ESCHERICHIA COLI ENOYL REDUCTASE WITH BOUND NAD AND THIENO-DIAZABORINE Deposited 1997-01-16	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–261（261 aa） Chain B 1–261（261 aa）	Not recorded	NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 TDB 6-METHYL-2(PROPANE-1-SULFONYL)-2H-THIENO[3,2-D][1,2,3]DIAZABORININ-1-OL × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；15% PEG 400, PH5.0 100MM ACETATE, 5MM NAD, 5MM 1,2-DIHYDRO-1-HYDROXY-2-(PROP-1-YLSULPHONYL)(5- METHYLTHIENO)[3,2-E][1,2,3]DIAZABORINE	Resolution 2.20 Å
1DFI X-RAY STRUCTURE OF ESCHERICHIA COLI ENOYL REDUCTASE WITH BOUND NAD Deposited 1997-01-16	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–261（261 aa） Chain B 1–261（261 aa） Chain C 1–261（261 aa） Chain D 1–261（261 aa）	Not recorded	NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；12% PEG 400, PH 5.0 ACETATE, 10MM NAD	Resolution 2.09 Å
1I2Z E. COLI ENOYL REDUCTASE IN COMPLEX WITH NAD AND BRL-12654 Deposited 2001-02-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 0–261（262 aa） Chain B 0–261（262 aa）	Not recorded	NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 654 4-(2-THIENYL)-1-(4-METHYLBENZYL)-1H-IMIDAZOLE × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å R-free 0.273
1I30 E. Coli Enoyl Reductase +NAD+SB385826 Deposited 2001-02-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 0–261（262 aa） Chain B 0–261（262 aa）	Not recorded	NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 826 1,3,4,9-TETRAHYDRO-2-(HYDROXYBENZOYL)-9-[(4-HYDROXYPHENYL)METHYL]-6-METHOXY-2H-PYRIDO[3,4-B]INDOLE × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.40 Å R-free 0.277
1LX6 Crystal Structure of E. Coli Enoyl Reductase-NAD+ with a Bound Benzamide Inhibitor Deposited 2002-06-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 0–261（262 aa） Chain B 0–261（262 aa）	Not recorded	NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 ZAM 3-[(ACETYL-METHYL-AMINO)-METHYL]-4-AMINO-N-METHYL-N-(1-METHYL-1H-INDOL-2-YLMETHYL)-BENZAMIDE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；298 K；0.1M HEPES, 2M(NH4)2SO4,5% PEG400, pH 7.50, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 2.40 Å R-free 0.250
1LXC Crystal Structure of E. Coli Enoyl Reductase-NAD+ with a Bound Acrylamide Inhibitor Deposited 2002-06-05	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 0–261（262 aa） Chain B 0–261（262 aa）	Not recorded	NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 AYM 3-(6-AMINOPYRIDIN-3-YL)-N-METHYL-N-[(1-METHYL-1H-INDOL-2-YL)METHYL]ACRYLAMIDE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；298 K；0.1 M HEPES, 2M(NH4)2SO4,5% PEG400, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 2.40 Å R-free 0.253
1MFP E. coli Enoyl Reductase in complex with NAD and SB611113 Deposited 2002-08-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 0–261（262 aa） Chain B 0–261（262 aa）	Not recorded	NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 IDN (E)-N-METHYL-N-(1-METHYL-1H-INDOL-3-YLMETHYL)-3-(7-OXO-5,6,7,8-TETRAHYDRO-[1,8]NAPHTHYRIDIN-3-YL)-ACRYLAMIDE × 4 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；294 K；NAD+, HEPES, ammonium sulfate, PEG 400, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 294.0K	Resolution 2.33 Å R-free 0.259
1QG6 CRYSTAL STRUCTURE OF E. COLI ENOYL ACYL CARRIER PROTEIN REDUCTASE IN COMPLEX WITH NAD AND TRICLOSAN Deposited 1999-04-20	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–261（261 aa） Chain B 1–261（261 aa） Chain C 1–261（261 aa） Chain D 1–261（261 aa）	Not recorded	NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 TCL TRICLOSAN × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 5；HANGING DROPS WERE FORMED BY MIXING 4MICROLITRES OF COMPLEX SOLUTION (15MG/ML PROTEIN, 3MM NADH, 0.6MM TRICLOSAN) WITH 4 MICROLITRES OF A RESERVOIR SOLUTION CONTAINING 12-16% (W/V) PEG 400 AND 0.1M SODIUM ACETATE PH 4.8-5.2 AT ROOM TEMPERATURE, pH 5.0	Resolution 1.90 Å R-free 0.207

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	FABI_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–265； UniProt 1–262 Author chain B； PDBConstruct 4–265； UniProt 1–262 Author chain C； PDBConstruct 4–265； UniProt 1–262 Author chain D； PDBConstruct 4–265； UniProt 1–262 Author chain E； PDBConstruct 4–265； UniProt 1–262 Author chain F； PDBConstruct 4–265； UniProt 1–262 Author chain G； PDBConstruct 4–265； UniProt 1–262 Author chain H； PDBConstruct 4–265； UniProt 1–262

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.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1qsg
Deposition date deposition_date	1999-06-21
Structure title title	CRYSTAL STRUCTURE OF ENOYL REDUCTASE INHIBITION BY TRICLOSAN
Keywords keywords	ENOYL REDUCTASE, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method method	X-RAY DIFFRACTION

▼

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

Radius of gyration Rg (Guinier) rg_guinier	46.12 Å
Radius of gyration Rg (electron density) rg_electron	46.30 Å
Forward intensity I(0) i0	789070000.00
Molecular weight molecular_weight	227920.0 kDa
Excluded volume excluded_volume	282890 Å³
Envelope volume envelope_volume	354980 Å³
Hydration-shell volume shell_volume	64217 Å³
Envelope diameter envelope_diameter	163.9 Å
Shell Rg shell_rg	49.88 Å
Envelope Rg envelope_rg	45.97 Å
Shape Rg shape_rg	46.31 Å
Total Rg total_rg	46.42 Å
Total atoms total_atoms	15937
Residues n_residues	2065
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

▼

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

Maximum dimension Dmax dmax	156.3 Å
Rg (real space) rg_real	46.43 Å
Rg uncertainty (real space) rg_real_error	1.65 Å
I(0) (real space) i0_real	7.8910e+08
I(0) uncertainty (real space) i0_real_error	1.4530e+07
Rg (reciprocal space) rg_reciprocal	46.12 Å
I(0) (reciprocal space) i0_reciprocal	788800000.0000
Solution quality estimate total_estimate	0.8340
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	41.4 Å
Skewness Skewness skewness	0.424
Kurtosis Kurtosis kurtosis	-0.605
Angular range angular_range	— – 0.1700 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	123300000.0000
Real-space data points n_real_points	35
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.723; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.939; Smooth: 0.730

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE
Molecular weight formula_weight	28175.2 kDa
EC 编号 ec_number	1.3.1.9
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H
Atom count atom_count	17287

GSHMGFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQNDKLKGRVEEFAAQLGSDIVLQCDVAEDASIDTMFAELGKVWPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKIAHDISSYSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYNVMGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIKDFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGISGEVVHVDGGFSIAAMNELELK

来源 Source

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	562
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	alpha-D-glucopyranose
Molecular weight formula_weight	180.2 kDa
Source method src_method	man
Copy count entity_count	8

Entity 3 Entity 3 non-polymer

Description description	NICOTINAMIDE-ADENINE-DINUCLEOTIDE
Molecular weight formula_weight	663.4 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 4 Entity 4 non-polymer

Description description	TRICLOSAN
Molecular weight formula_weight	289.5 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1350

▼

7. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (16 domains)

Domain ID domain_id	d1qsga1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamily	c.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family family	c.2.1.2 — Tyrosine-dependent oxidoreductases

Domain ID domain_id	d1qsga2
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	d1qsgb1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamily	c.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family family	c.2.1.2 — Tyrosine-dependent oxidoreductases

Domain ID domain_id	d1qsgb2
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	d1qsgc1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamily	c.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family family	c.2.1.2 — Tyrosine-dependent oxidoreductases

Domain ID domain_id	d1qsgc2
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	d1qsgd1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamily	c.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family family	c.2.1.2 — Tyrosine-dependent oxidoreductases

Domain ID domain_id	d1qsgd2
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	d1qsge1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamily	c.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family family	c.2.1.2 — Tyrosine-dependent oxidoreductases

Domain ID domain_id	d1qsge2
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	d1qsgf1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamily	c.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family family	c.2.1.2 — Tyrosine-dependent oxidoreductases

Domain ID domain_id	d1qsgf2
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	d1qsgg1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamily	c.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family family	c.2.1.2 — Tyrosine-dependent oxidoreductases

Domain ID domain_id	d1qsgg2
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	d1qsgh1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamily	c.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family family	c.2.1.2 — Tyrosine-dependent oxidoreductases

Domain ID domain_id	d1qsgh2
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

CATH v4.4 (8 domains)

Domain ID domain_id	1qsgA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	720 — NAD(P)-binding Rossmann-like Domain

Domain ID domain_id	1qsgB00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	720 — NAD(P)-binding Rossmann-like Domain

Domain ID domain_id	1qsgC00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	720 — NAD(P)-binding Rossmann-like Domain

Domain ID domain_id	1qsgD00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	720 — NAD(P)-binding Rossmann-like Domain

Domain ID domain_id	1qsgE00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	720 — NAD(P)-binding Rossmann-like Domain

Domain ID domain_id	1qsgF00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	720 — NAD(P)-binding Rossmann-like Domain

Domain ID domain_id	1qsgG00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	720 — NAD(P)-binding Rossmann-like Domain

Domain ID domain_id	1qsgH00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	720 — NAD(P)-binding Rossmann-like Domain

▶

8. Citations (1)

▶

Unit-cell length a length_a	73.733 Å
Unit-cell length b length_b	82.077 Å
Unit-cell length c length_c	84.177 Å
Unit-cell angle α angle_alpha	89.54 °
Unit-cell angle β angle_beta	87.43 °
Unit-cell angle γ angle_gamma	77.77 °
Molecules per unit cell Z z_pdb	8

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

Resolution resolution	1.750 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	—
R_work r_work	0.1720
R_free r_free	0.2150

fit	/app/data/saxs_computation/qs/1qsg/1qsg.fit
pddf	/app/data/pr_computation/qs/1qsg/1qsg.pr.out
profile	/app/data/saxs_computation/qs/1qsg/1qsg.dat