SAXSdb — 1fvq

▼

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

COPPER-TRANSPORTING ATPASE

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 1–72	Fragment：CCC2A DOMAIN	No other associated polymer	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

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 1FVQ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1FVS SOLUTION STRUCTURE OF THE YEAST COPPER TRANSPORTER DOMAIN CCC2A IN THE APO AND CU(I) LOAD STATES Deposited 2000-09-20	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
2GGP Solution structure of the Atx1-Cu(I)-Ccc2a complex Deposited 2006-03-24	Different construct Different oligomeric state Different ligand/ion Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 2–72（71 aa） Fragment：HMA 1 domain, residues 2-72	Not recorded	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

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	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–72； UniProt 1–72

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1fvq
Deposition date deposition_date	2000-09-20
Structure title title	SOLUTION STRUCTURE OF THE YEAST COPPER TRANSPORTER DOMAIN CCC2A IN THE APO AND CU(I) LOADED STATES
Keywords keywords	APO-Ccc2a, HYDROLASE; HYDROLASE
Experimental Method method	SOLUTION NMR

▼

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

Radius of gyration Rg (Guinier) rg_guinier	12.45 Å
Radius of gyration Rg (electron density) rg_electron	10.92 Å
Forward intensity I(0) i0	1546940.00
Molecular weight molecular_weight	7877.0 kDa
Excluded volume excluded_volume	9643 Å³
Envelope volume envelope_volume	10522 Å³
Hydration-shell volume shell_volume	8388 Å³
Envelope diameter envelope_diameter	36.8 Å
Shell Rg shell_rg	16.38 Å
Envelope Rg envelope_rg	11.25 Å
Shape Rg shape_rg	10.91 Å
Total Rg total_rg	12.29 Å
Total atoms total_atoms	1084
Residues n_residues	72
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	38.9 Å
Rg (real space) rg_real	12.36 Å
Rg uncertainty (real space) rg_real_error	0.23 Å
I(0) (real space) i0_real	1.5470e+06
I(0) uncertainty (real space) i0_real_error	1.6520e+04
Rg (reciprocal space) rg_reciprocal	12.37 Å
I(0) (reciprocal space) i0_reciprocal	1547000.0000
Solution quality estimate total_estimate	0.8780
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	16.2 Å
Skewness Skewness skewness	0.127
Kurtosis Kurtosis kurtosis	-0.271
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	369300.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.860; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.845

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (1)

▼

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1fvqa1
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	d1fvqa2
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 (1 domains)

Domain ID domain_id	1fvqA00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	100 —

▶

8. Citations (1)

▶

Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

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

Description description	COPPER-TRANSPORTING ATPASE
Molecular weight formula_weight	7889.9 kDa
EC 编号 ec_number	3.6.1.36
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1084

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

SOLUTION STRUCTURE OF THE YEAST COPPER TRANSPORTER DOMAIN CCC2A IN THE APO AND CU(I) LOADED STATES

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

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

Unit cell Unit Cell

Symmetry Symmetry

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/fv/1fvq/1fvq.fit
pddf	/app/data/pr_computation/fv/1fvq/1fvq.pr.out
profile	/app/data/saxs_computation/fv/1fvq/1fvq.dat