SAXSdb — 2ggp

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

Metal homeostasis factor ATX1

Saccharomyces cerevisiae

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–73	Fragment：HMA domain, residues 1-73	Probable copper-transporting ATPase × 1 （P38995） CU1 COPPER (I) ION × 1	SOLUTION NMR NMR measurement conditions：pH 7；298 K；Ionic strength (raw mmCIF value) 100 mM KPi；Pressure ambient NMR sample composition：1mM Atx1 U-15N,13C, 1mM Ccc2a unlabeled, 1mM Cu(I), 100mM KPi, 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided

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 2GGP	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CC7 CRYSTAL STRUCTURE OF THE ATX1 METALLOCHAPERONE PROTEIN Deposited 1999-03-04	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–73（73 aa）	Not recorded	BEN BENZAMIDINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；pH 6.0	Resolution 1.20 Å R-free 0.211
1CC8 CRYSTAL STRUCTURE OF THE ATX1 METALLOCHAPERONE PROTEIN Deposited 1999-03-04	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–73（73 aa）	Not recorded	HG MERCURY (II) ION × 1 BEN BENZAMIDINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；pH 6.0	Resolution 1.02 Å R-free 0.172
1FD8 SOLUTION STRUCTURE OF THE CU(I) FORM OF THE YEAST METALLOCHAPERONE, ATX1 Deposited 2000-07-20	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–73（73 aa）	Not recorded	CU1 COPPER (I) ION × 1	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 100mM phosphate；Pressure ambient NMR sample composition 1.8mM Cu(I)-Atx1 15N; 100mM phosphate buffer NA; 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
1FES SOLUTION STRUCTURE OF THE APO FORM OF THE YEAST METALLOCHAPERONE, ATX1 Deposited 2000-07-22	Different construct Different oligomeric state Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–73（73 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 100mM phosphate；Pressure ambient NMR sample composition 1.8mM Apo-Atx1 15N; 100mM phosphate buffer NA; 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
3K7R Crystal structure of [TM][CuAtx1]3 Deposited 2009-10-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–73（73 aa） Chain B 1–73（73 aa） Chain C 1–73（73 aa）	Not recorded	CU COPPER (II) ION × 4 4SM TETRATHIOMOLYBDATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 7；287 K；0.15 M DL-Malic acid, pH 7.0, 20% PEG 3350, EVAPORATION, temperature 287K	Resolution 2.28 Å R-free 0.256
3K7R Crystal structure of [TM][CuAtx1]3 Deposited 2009-10-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain D 1–73（73 aa） Chain E 1–73（73 aa） Chain F 1–73（73 aa）	Not recorded	CU COPPER (II) ION × 4 4SM TETRATHIOMOLYBDATE × 1 MLT D-MALATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 7；287 K；0.15 M DL-Malic acid, pH 7.0, 20% PEG 3350, EVAPORATION, temperature 287K	Resolution 2.28 Å R-free 0.256
3K7R Crystal structure of [TM][CuAtx1]3 Deposited 2009-10-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain G 1–73（73 aa） Chain H 1–73（73 aa） Chain I 1–73（73 aa）	Not recorded	CU COPPER (II) ION × 4 4SM TETRATHIOMOLYBDATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 7；287 K；0.15 M DL-Malic acid, pH 7.0, 20% PEG 3350, EVAPORATION, temperature 287K	Resolution 2.28 Å R-free 0.256
3K7R Crystal structure of [TM][CuAtx1]3 Deposited 2009-10-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain J 1–73（73 aa） Chain K 1–73（73 aa） Chain L 1–73（73 aa）	Not recorded	CU COPPER (II) ION × 4 4SM TETRATHIOMOLYBDATE × 1 MLT D-MALATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 7；287 K；0.15 M DL-Malic acid, pH 7.0, 20% PEG 3350, EVAPORATION, temperature 287K	Resolution 2.28 Å R-free 0.256
3K7R Crystal structure of [TM][CuAtx1]3 Deposited 2009-10-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–73（73 aa） Chain B 1–73（73 aa） Chain C 1–73（73 aa） Chain D 1–73（73 aa） Chain E 1–73（73 aa） Chain F 1–73（73 aa）	Not recorded	CU COPPER (II) ION × 8 4SM TETRATHIOMOLYBDATE × 2 MLT D-MALATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 7；287 K；0.15 M DL-Malic acid, pH 7.0, 20% PEG 3350, EVAPORATION, temperature 287K	Resolution 2.28 Å R-free 0.256
3K7R Crystal structure of [TM][CuAtx1]3 Deposited 2009-10-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 6 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain G 1–73（73 aa） Chain H 1–73（73 aa） Chain I 1–73（73 aa） Chain J 1–73（73 aa） Chain K 1–73（73 aa） Chain L 1–73（73 aa）	Not recorded	CU COPPER (II) ION × 8 4SM TETRATHIOMOLYBDATE × 2 MLT D-MALATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 7；287 K；0.15 M DL-Malic acid, pH 7.0, 20% PEG 3350, EVAPORATION, temperature 287K	Resolution 2.28 Å R-free 0.256
5VDE Crystal Structure of Cu(I)-loaded yeast Atx1: Crystal Form I Deposited 2017-04-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–73（73 aa） Chain B 1–73（73 aa）	Not recorded	CU1 COPPER (I) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.3；293 K；0.1 M HEPES (pH 7.3), 24% (W/v) PEG3350	Resolution 1.65 Å R-free 0.206
5VDE Crystal Structure of Cu(I)-loaded yeast Atx1: Crystal Form I Deposited 2017-04-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–73（73 aa） Chain D 1–73（73 aa）	Not recorded	CU1 COPPER (I) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.3；293 K；0.1 M HEPES (pH 7.3), 24% (W/v) PEG3350	Resolution 1.65 Å R-free 0.206
5VDE Crystal Structure of Cu(I)-loaded yeast Atx1: Crystal Form I Deposited 2017-04-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–73（73 aa） Chain B 1–73（73 aa） Chain C 1–73（73 aa） Chain D 1–73（73 aa）	Not recorded	CU1 COPPER (I) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.3；293 K；0.1 M HEPES (pH 7.3), 24% (W/v) PEG3350	Resolution 1.65 Å R-free 0.206
5VDF Crystal Structure of Cu(I)-loaded yeast Atx1: Crystal Form II Deposited 2017-04-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–73（73 aa） Chain B 1–73（73 aa）	Not recorded	CU1 COPPER (I) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.9；293 K；0.1 M HEPES (pH 7.9), 20% (w/v) PEG3350	Resolution 1.93 Å R-free 0.242
5VDF Crystal Structure of Cu(I)-loaded yeast Atx1: Crystal Form II Deposited 2017-04-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–73（73 aa） Chain D 1–73（73 aa）	Not recorded	CU1 COPPER (I) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.9；293 K；0.1 M HEPES (pH 7.9), 20% (w/v) PEG3350	Resolution 1.93 Å R-free 0.242
5VDF Crystal Structure of Cu(I)-loaded yeast Atx1: Crystal Form II Deposited 2017-04-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain E 1–73（73 aa） Chain F 1–73（73 aa）	Not recorded	CU1 COPPER (I) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.9；293 K；0.1 M HEPES (pH 7.9), 20% (w/v) PEG3350	Resolution 1.93 Å R-free 0.242
5VDF Crystal Structure of Cu(I)-loaded yeast Atx1: Crystal Form II Deposited 2017-04-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain G 1–73（73 aa） Chain H 1–73（73 aa）	Not recorded	CU1 COPPER (I) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.9；293 K；0.1 M HEPES (pH 7.9), 20% (w/v) PEG3350	Resolution 1.93 Å R-free 0.242
5VDF Crystal Structure of Cu(I)-loaded yeast Atx1: Crystal Form II Deposited 2017-04-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–73（73 aa） Chain B 1–73（73 aa）	Not recorded	CU1 COPPER (I) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.9；293 K；0.1 M HEPES (pH 7.9), 20% (w/v) PEG3350	Resolution 1.93 Å R-free 0.242
5VDF Crystal Structure of Cu(I)-loaded yeast Atx1: Crystal Form II Deposited 2017-04-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 6 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–73（73 aa） Chain D 1–73（73 aa）	Not recorded	CU1 COPPER (I) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.9；293 K；0.1 M HEPES (pH 7.9), 20% (w/v) PEG3350	Resolution 1.93 Å R-free 0.242
5VDF Crystal Structure of Cu(I)-loaded yeast Atx1: Crystal Form II Deposited 2017-04-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 7 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain G 1–73（73 aa） Chain H 1–73（73 aa）	Not recorded	CU1 COPPER (I) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.9；293 K；0.1 M HEPES (pH 7.9), 20% (w/v) PEG3350	Resolution 1.93 Å R-free 0.242

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

View Construct and Data Evidence

UniProt name	ATX1_YEAST
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–73； UniProt 1–73

Probable copper-transporting ATPase

Saccharomyces cerevisiae

UniProt P38995

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 2–72	Fragment：HMA 1 domain, residues 2-72	Metal homeostasis factor ATX1 × 1 （P38636） CU1 COPPER (I) ION × 1	SOLUTION NMR NMR measurement conditions：pH 7；298 K；Ionic strength (raw mmCIF value) 100 mM KPi；Pressure ambient NMR sample composition：1mM Atx1 U-15N,13C, 1mM Ccc2a unlabeled, 1mM Cu(I), 100mM KPi, 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided

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 2GGP	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1FVQ SOLUTION STRUCTURE OF THE YEAST COPPER TRANSPORTER DOMAIN CCC2A IN THE APO AND CU(I) LOADED STATES Deposited 2000-09-20	Different construct Different oligomeric state Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–72（72 aa） Fragment：CCC2A DOMAIN	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 100mM phosphate；Pressure ambient NMR sample composition 2.2mM apo-Ccc2a(15N); 100mM phosphate buffer NA \| 90% H2O/10% D2O	Resolution not provided
1FVS SOLUTION STRUCTURE OF THE YEAST COPPER TRANSPORTER DOMAIN CCC2A IN THE APO AND CU(I) LOAD STATES Deposited 2000-09-20	Different construct Different oligomeric state Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–72（72 aa） Fragment：CCC2A DOMAIN	Not recorded	CU COPPER (II) ION × 1	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 100mM phosphate；Pressure ambient NMR sample composition 1.2mM Cu(I)-Ccc2a; 100mM phosphate buffer \| 90% H2O/10% D2O	Resolution not provided

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ATU2_YEAST
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 2–72； UniProt 2–72

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	2ggp
Deposition date deposition_date	2006-03-24
Structure title title	Solution structure of the Atx1-Cu(I)-Ccc2a complex
Keywords keywords	Copper transport, complex, Structural Genomics, Structural Proteomics in Europe, SPINE, CHAPERONE, METAL TRANSPORT; CHAPERONE, METAL TRANSPORT
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	16.69 Å
Radius of gyration Rg (electron density) rg_electron	16.65 Å
Forward intensity I(0) i0	1485170000.00
Molecular weight molecular_weight	323260.0 kDa
Excluded volume excluded_volume	403400 Å³
Envelope volume envelope_volume	38320 Å³
Hydration-shell volume shell_volume	17574 Å³
Envelope diameter envelope_diameter	64.3 Å
Shell Rg shell_rg	24.78 Å
Envelope Rg envelope_rg	19.21 Å
Shape Rg shape_rg	16.66 Å
Total Rg total_rg	16.73 Å
Total atoms total_atoms	45300
Residues n_residues	2900
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	60.4 Å
Rg (real space) rg_real	16.74 Å
Rg uncertainty (real space) rg_real_error	0.50 Å
I(0) (real space) i0_real	1.4850e+09
I(0) uncertainty (real space) i0_real_error	1.9290e+07
Rg (reciprocal space) rg_reciprocal	16.74 Å
I(0) (reciprocal space) i0_reciprocal	1485000000.0000
Solution quality estimate total_estimate	0.8082
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	17.2 Å
Skewness Skewness skewness	0.420
Kurtosis Kurtosis kurtosis	-0.307
Angular range angular_range	— – 0.4750 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	899800.0000
Real-space data points n_real_points	78
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.544; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.871; Smooth: 1.000

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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	Metal homeostasis factor ATX1
Molecular weight formula_weight	8232.6 kDa
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	45300

MAEIKHYQFNVVMTCSGCSGAVNKVLTKLEPDVSKIDISLEKQLVDVYTTLPYDFILEKIKKTGKEVRSGKQL

来源 Source

来源生物 organism	Saccharomyces cerevisiae
通用名 common_name	;baker's yeast ;
NCBI Class编号 ncbi_taxonomy_id	4932
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	Probable copper-transporting ATPase
Molecular weight formula_weight	7889.9 kDa
EC 编号 ec_number	3.6.3.4
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

AREVILAVHGMTCSACTNTINTQLRALKGVTKCDISLVTNECQVTYDNEVTADSIKEIIEDCGFDCEILRDS

来源 Source

来源生物 organism	Saccharomyces cerevisiae
通用名 common_name	;baker's yeast ;
NCBI Class编号 ncbi_taxonomy_id	4932
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 3 Entity 3 non-polymer

Description description	COPPER (I) ION
Molecular weight formula_weight	63.5 kDa
Source method src_method	syn
Copy count entity_count	1

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7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d2ggpa_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.58 — Ferredoxin-like
Superfamily Superfamily superfamily	d.58.17 — HMA, heavy metal-associated domain
Family Family family	d.58.17.1 — HMA, heavy metal-associated domain

Domain ID domain_id	d2ggpb2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.58 — Ferredoxin-like
Superfamily Superfamily superfamily	d.58.17 — HMA, heavy metal-associated domain
Family Family family	d.58.17.1 — HMA, heavy metal-associated domain

Domain ID domain_id	d2ggpb3
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 (2 domains)

Domain ID domain_id	2ggpA00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	100 —

Domain ID domain_id	2ggpB00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	100 —

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8. Citations (1)

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fit	/app/data/saxs_computation/gg/2ggp/2ggp.fit
pddf	/app/data/pr_computation/gg/2ggp/2ggp.pr.out
profile	/app/data/saxs_computation/gg/2ggp/2ggp.dat

Solution structure of the Atx1-Cu(I)-Ccc2a complex

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

Metal homeostasis factor ATX1

State in the Current Structure

Other States of the Same Protein in the Database

Probable copper-transporting ATPase

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

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)