SAXSdb — 5ecs

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

Glutathione S-transferase U20

Arabidopsis thaliana

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 1–217	Not recorded	GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8.5；297 K；0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl, 30%(w/v) PEG 3000	Resolution 1.65 Å R-free 0.188
2	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 1–217	Not recorded	GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 8.5；297 K；0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl, 30%(w/v) PEG 3000	Resolution 1.65 Å R-free 0.188

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 5ECS	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5ECH Crystal Structure of FIN219-FIP1 complex with JA and ATP Deposited 2015-10-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–217（217 aa） Chain C 1–217（217 aa）	Not recorded	JAA {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetic acid × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；297 K；0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl, 30%(w/v) PEG 3000	Resolution 2.14 Å R-free 0.180
5ECH Crystal Structure of FIN219-FIP1 complex with JA and ATP Deposited 2015-10-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 1–217（217 aa） Chain F 1–217（217 aa）	Not recorded	JAA {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetic acid × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；297 K；0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl, 30%(w/v) PEG 3000	Resolution 2.14 Å R-free 0.180
5ECI Crystal Structure of FIN219-FIP1 complex with JA, ATP and Mg Deposited 2015-10-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–217（217 aa） Chain C 1–217（217 aa）	Not recorded	JAA {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetic acid × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；297 K；0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl, 30%(w/v) PEG 3000	Resolution 1.56 Å R-free 0.225
5ECI Crystal Structure of FIN219-FIP1 complex with JA, ATP and Mg Deposited 2015-10-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 1–217（217 aa） Chain F 1–217（217 aa）	Not recorded	JAA {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetic acid × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；297 K；0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl, 30%(w/v) PEG 3000	Resolution 1.56 Å R-free 0.225
5ECK Crystal Structure of FIN219-FIP1 complex with JA, Ile and ATP Deposited 2015-10-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–217（217 aa） Chain C 1–217（217 aa）	Not recorded	ILE ISOLEUCINE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 JAA {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetic acid × 1 GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；297 K；0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl, 30%(w/v) PEG 3000	Resolution 1.54 Å R-free 0.175
5ECK Crystal Structure of FIN219-FIP1 complex with JA, Ile and ATP Deposited 2015-10-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 1–217（217 aa） Chain F 1–217（217 aa）	Not recorded	ILE ISOLEUCINE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 JAA {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetic acid × 1 GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；297 K；0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl, 30%(w/v) PEG 3000	Resolution 1.54 Å R-free 0.175
5ECL Crystal Structure of FIN219-FIP1 complex with JA, Ile and Mg Deposited 2015-10-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–217（217 aa） Chain C 1–217（217 aa）	Not recorded	JAA {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetic acid × 1 ILE ISOLEUCINE × 1 MG MAGNESIUM ION × 1 GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；297 K；0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl, 30%(w/v) PEG 3000	Resolution 1.85 Å R-free 0.219
5ECL Crystal Structure of FIN219-FIP1 complex with JA, Ile and Mg Deposited 2015-10-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 1–217（217 aa） Chain F 1–217（217 aa）	Not recorded	JAA {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetic acid × 1 ILE ISOLEUCINE × 1 MG MAGNESIUM ION × 3 GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；297 K；0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl, 30%(w/v) PEG 3000	Resolution 1.85 Å R-free 0.219
5ECM Crystal Structure of FIN219-FIP1 complex with JA and Leu Deposited 2015-10-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–217（217 aa） Chain C 1–217（217 aa）	Not recorded	JAA {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetic acid × 1 LEU LEUCINE × 1 GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；297 K；0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl, 30%(w/v) PEG 3000	Resolution 1.60 Å R-free 0.245
5ECM Crystal Structure of FIN219-FIP1 complex with JA and Leu Deposited 2015-10-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 1–217（217 aa） Chain F 1–217（217 aa）	Not recorded	JAA {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetic acid × 1 LEU LEUCINE × 1 GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；297 K；0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl, 30%(w/v) PEG 3000	Resolution 1.60 Å R-free 0.245
5ECN Crystal Structure of FIN219-FIP1 complex with JA, Leu and ATP Deposited 2015-10-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–217（217 aa） Chain C 1–217（217 aa）	Not recorded	JAA {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetic acid × 1 LEU LEUCINE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；297 K；0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl, 30%(w/v) PEG 3000	Resolution 1.72 Å R-free 0.188
5ECN Crystal Structure of FIN219-FIP1 complex with JA, Leu and ATP Deposited 2015-10-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 1–217（217 aa） Chain F 1–217（217 aa）	Not recorded	JAA {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetic acid × 1 LEU LEUCINE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；297 K；0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl, 30%(w/v) PEG 3000	Resolution 1.72 Å R-free 0.188
5ECO Crystal Structure of FIN219-FIP1 complex with JA, Leu and Mg Deposited 2015-10-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–217（217 aa） Chain C 1–217（217 aa）	Not recorded	JAA {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetic acid × 1 LEU LEUCINE × 1 MG MAGNESIUM ION × 1 GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；297 K；0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl, 30%(w/v) PEG 3000	Resolution 1.80 Å R-free 0.239
5ECO Crystal Structure of FIN219-FIP1 complex with JA, Leu and Mg Deposited 2015-10-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 1–217（217 aa） Chain F 1–217（217 aa）	Not recorded	JAA {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetic acid × 1 LEU LEUCINE × 1 GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；297 K；0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl, 30%(w/v) PEG 3000	Resolution 1.80 Å R-free 0.239
5ECP Crystal Structure of FIN219-FIP1 complex with JA, MET and ATP Deposited 2015-10-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–217（217 aa） Chain C 1–217（217 aa）	Not recorded	JAA {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetic acid × 1 MET METHIONINE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；297 K；0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl, 30%(w/v) PEG 3000	Resolution 2.25 Å R-free 0.208
5ECP Crystal Structure of FIN219-FIP1 complex with JA, MET and ATP Deposited 2015-10-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 1–217（217 aa） Chain F 1–217（217 aa）	Not recorded	JAA {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetic acid × 1 MET METHIONINE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；297 K；0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl, 30%(w/v) PEG 3000	Resolution 2.25 Å R-free 0.208
5ECQ Crystal Structure of FIN219-FIP1 complex with JA, VAL and ATP Deposited 2015-10-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–217（217 aa） Chain C 1–217（217 aa）	Not recorded	JAA {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetic acid × 1 VAL VALINE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；297 K；0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl, 30%(w/v) PEG 3000	Resolution 1.66 Å R-free 0.234
5ECQ Crystal Structure of FIN219-FIP1 complex with JA, VAL and ATP Deposited 2015-10-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 1–217（217 aa） Chain F 1–217（217 aa）	Not recorded	JAA {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetic acid × 1 VAL VALINE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；297 K；0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl, 30%(w/v) PEG 3000	Resolution 1.66 Å R-free 0.234
5ECR Crystal Structure of FIN219-FIP1 complex with JA, VAL and Mg Deposited 2015-10-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–217（217 aa） Chain C 1–217（217 aa）	Not recorded	JAA {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetic acid × 1 VAL VALINE × 1 GSH Glutathione × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；297 K；0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl, 30%(w/v) PEG 3000	Resolution 1.72 Å R-free 0.281
5ECR Crystal Structure of FIN219-FIP1 complex with JA, VAL and Mg Deposited 2015-10-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 1–217（217 aa） Chain F 1–217（217 aa）	Not recorded	JAA {(1R,2R)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetic acid × 1 VAL VALINE × 1 GSH Glutathione × 2 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；297 K；0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl, 30%(w/v) PEG 3000	Resolution 1.72 Å R-free 0.281

10 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	GSTUK_ARATH
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 7–223； UniProt 1–217 Author chain B； PDBConstruct 7–223； UniProt 1–217

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	5ecs
Deposition date deposition_date	2015-10-20
Structure title title	Crystal Structure of FIP1 with GSH
Keywords keywords	Glutathione S-transferase, TRANSFERASE; TRANSFERASE
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	27.85 Å
Radius of gyration Rg (electron density) rg_electron	27.52 Å
Forward intensity I(0) i0	38592400.00
Molecular weight molecular_weight	49955.0 kDa
Excluded volume excluded_volume	63129 Å³
Envelope volume envelope_volume	75542 Å³
Hydration-shell volume shell_volume	24458 Å³
Envelope diameter envelope_diameter	96.3 Å
Shell Rg shell_rg	32.70 Å
Envelope Rg envelope_rg	27.67 Å
Shape Rg shape_rg	27.51 Å
Total Rg total_rg	28.13 Å
Total atoms total_atoms	3536
Residues n_residues	428
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	93.3 Å
Rg (real space) rg_real	28.13 Å
Rg uncertainty (real space) rg_real_error	0.77 Å
I(0) (real space) i0_real	3.8590e+07
I(0) uncertainty (real space) i0_real_error	5.8890e+05
Rg (reciprocal space) rg_reciprocal	28.05 Å
I(0) (reciprocal space) i0_reciprocal	38590000.0000
Solution quality estimate total_estimate	0.8346
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	24.6 Å
Skewness Skewness skewness	0.507
Kurtosis Kurtosis kurtosis	-0.471
Angular range angular_range	— – 0.2850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	12650000.0000
Real-space data points n_real_points	58
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.729; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.762; Smooth: 0.898

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Glutathione S-transferase U20
Molecular weight formula_weight	25867.3 kDa
EC 编号 ec_number	2.5.1.18
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	3804

HHHHHHMANLPILLDYWPSMFGMRARVALREKGVEFEYREEDFSNKSPLLLQSNPIHKKIPVLVHNGKPVCESLNVVQYVDEAWPEKNPFFPSDPYGRAQARFWADFVDKKFTDAQFKVWGKKGEEQEAGKKEFIEAVKILESELGDKPYFGGDSFGYVDISLITFSSWFQAYEKFGNFSIESESPKLIAWAKRCMEKESVSKSLPDSEKIVAYAAEYRKNNL

来源 Source

来源生物 organism	Arabidopsis thaliana
通用名 common_name	Mouse-ear cress
NCBI Class编号 ncbi_taxonomy_id	3702
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	GLUTATHIONE
Molecular weight formula_weight	307.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	268

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d5ecsa1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.47 — Thioredoxin fold
Superfamily Superfamily superfamily	c.47.1 — Thioredoxin-like
Family Family family	c.47.1.0 — automated matches

Domain ID domain_id	d5ecsa2
Class class	a — All alpha proteins
Fold Fold fold	a.45 — GST C-terminal domain-like
Superfamily Superfamily superfamily	a.45.1 — GST C-terminal domain-like
Family Family family	a.45.1.0 — automated matches

Domain ID domain_id	d5ecsb1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.47 — Thioredoxin fold
Superfamily Superfamily superfamily	c.47.1 — Thioredoxin-like
Family Family family	c.47.1.0 — automated matches

Domain ID domain_id	d5ecsb2
Class class	a — All alpha proteins
Fold Fold fold	a.45 — GST C-terminal domain-like
Superfamily Superfamily superfamily	a.45.1 — GST C-terminal domain-like
Family Family family	a.45.1.0 — automated matches

CATH v4.4 (4 domains)

Domain ID domain_id	5ecsA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	30 — Glutaredoxin
Homologous superfamily homologous superfamily	10 — Glutaredoxin

Domain ID domain_id	5ecsA02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1050 — Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	5ecsB01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	30 — Glutaredoxin
Homologous superfamily homologous superfamily	10 — Glutaredoxin

Domain ID domain_id	5ecsB02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1050 — Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
Homologous superfamily homologous superfamily	10 —

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8. Citations (1)

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Unit-cell length a length_a	90.383 Å
Unit-cell length b length_b	58.893 Å
Unit-cell length c length_c	97.900 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	100.50 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	1.650 Å
Low-resolution limit resolution_low	26.650 Å
R factor r_factor	0.1709
R_work r_work	0.1703
R_free r_free	0.1880

fit	/app/data/saxs_computation/ec/5ecs/5ecs.fit
pddf	/app/data/pr_computation/ec/5ecs/5ecs.pr.out
profile	/app/data/saxs_computation/ec/5ecs/5ecs.dat

Crystal Structure of FIP1 with GSH

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

Glutathione S-transferase U20

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