SAXSdb — 1cpz

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

Copper chaperone

Enterococcus hirae

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 3–69	Mutation：N-TERMINUS CHANGED FROM MKQ TO AQ	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 7；288.2 K；Ionic strength (raw mmCIF value) 50 mM NMR sample composition：10% D2O/90% H2O, 10UM NA2S2O4, 50MM NAPI	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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	A0A1V8XBM5_ENTHR
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–68； UniProt 3–69

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	1cpz
Deposition date deposition_date	1999-05-06
Structure title title	COPPER CHAPERONE OF ENTEROCOCCUS HIRAE (APO-FORM)
Keywords keywords	COPPER CHAPERONE, METAL TRANSPORT, GENE REGULATION; GENE REGULATION
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	11.33 Å
Radius of gyration Rg (electron density) rg_electron	11.04 Å
Forward intensity I(0) i0	312765000.00
Molecular weight molecular_weight	148970.0 kDa
Excluded volume excluded_volume	186830 Å³
Envelope volume envelope_volume	15109 Å³
Hydration-shell volume shell_volume	10446 Å³
Envelope diameter envelope_diameter	40.8 Å
Shell Rg shell_rg	18.06 Å
Envelope Rg envelope_rg	12.63 Å
Shape Rg shape_rg	11.00 Å
Total Rg total_rg	11.35 Å
Total atoms total_atoms	21180
Residues n_residues	1360
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	35.5 Å
Rg (real space) rg_real	11.26 Å
Rg uncertainty (real space) rg_real_error	0.27 Å
I(0) (real space) i0_real	3.1280e+08
I(0) uncertainty (real space) i0_real_error	3.5020e+06
Rg (reciprocal space) rg_reciprocal	11.27 Å
I(0) (reciprocal space) i0_reciprocal	312800000.0000
Solution quality estimate total_estimate	0.7844
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	14.4 Å
Skewness Skewness skewness	0.138
Kurtosis Kurtosis kurtosis	-0.173
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	148900.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.737; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1cpza_
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

CATH v4.4 (1 domains)

Domain ID domain_id	1cpzA00
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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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 chaperone
Molecular weight formula_weight	7475.7 kDa
Mutation mutation	N-TERMINUS CHANGED FROM MKQ TO AQ
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	21180

来源生物 organism	Enterococcus hirae
NCBI Class编号 ncbi_taxonomy_id	1354
宿主生物 host_organism	Escherichia coli BL21

COPPER CHAPERONE OF ENTEROCOCCUS HIRAE (APO-FORM)

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

Copper chaperone

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) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/cp/1cpz/1cpz.fit
pddf	/app/data/pr_computation/cp/1cpz/1cpz.pr.out
profile	/app/data/saxs_computation/cp/1cpz/1cpz.dat