1co4

SOLUTION STRUCTURE OF A ZINC DOMAIN CONSERVED IN YEAST COPPER-REGULATED TRANSCRIPTION FACTORS

Method: SOLUTION NMR D_max: 51.0 Å Quality: REASONABLE

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

PROTEIN (ACTIVATOR OF METALLOTHIONEIN 1)

OrganismNot specified

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 1–42	Fragment：RESIDUES 1-42	ZN ZINC ION × 1	SOLUTION NMR NMR measurement conditions：pH 6.5；298 K；Ionic strength (raw mmCIF value) 25mM NACL NMR sample composition：25MM NAOAC, 0.1MM ZNCL2, 90% WATER/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.

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

View Construct and Data Evidence

UniProt name	AMT1_CANGA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–42； UniProt 1–42

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

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1co4
Deposition date deposition_date	1999-06-04
Structure title title	SOLUTION STRUCTURE OF A ZINC DOMAIN CONSERVED IN YEAST COPPER-REGULATED TRANSCRIPTION FACTORS
Keywords keywords	METALLOTHIONEIN, AMT, METAL REGULATION, TRANSLATION-REGULATION PROTEIN COMPLEX; TRANSLATION/REGULATION PROTEIN
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	11.65 Å
Radius of gyration Rg (electron density) rg_electron	11.52 Å
Forward intensity I(0) i0	81001300.00
Molecular weight molecular_weight	70949.0 kDa
Excluded volume excluded_volume	87617 Å³
Envelope volume envelope_volume	19906 Å³
Hydration-shell volume shell_volume	11442 Å³
Envelope diameter envelope_diameter	50.2 Å
Shell Rg shell_rg	20.59 Å
Envelope Rg envelope_rg	16.37 Å
Shape Rg shape_rg	11.56 Å
Total Rg total_rg	11.81 Å
Total atoms total_atoms	8850
Residues n_residues	630
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	51.0 Å
Rg (real space) rg_real	11.86 Å
Rg uncertainty (real space) rg_real_error	0.66 Å
I(0) (real space) i0_real	8.1000e+07
I(0) uncertainty (real space) i0_real_error	1.0990e+06
Rg (reciprocal space) rg_reciprocal	11.85 Å
I(0) (reciprocal space) i0_reciprocal	81000000.0000
Solution quality estimate total_estimate	0.6906
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	11.0 Å
Skewness Skewness skewness	0.635
Kurtosis Kurtosis kurtosis	-0.003
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	29800.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.313; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.036; Smooth: 0.999

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1co4a_
Class class	g — Small proteins
Fold Fold fold	g.47 — Zinc domain conserved in yeast copper-regulated transcription factors
Superfamily Superfamily superfamily	g.47.1 — Zinc domain conserved in yeast copper-regulated transcription factors
Family Family family	g.47.1.1 — Zinc domain conserved in yeast copper-regulated transcription factors

CATH v4.4 (1 domains)

Domain ID domain_id	1co4A00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	430 — Activator Of Metallothionein 1; Chain A
Homologous superfamily homologous superfamily	10 — Copper fist DNA-binding domain

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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	PROTEIN (ACTIVATOR OF METALLOTHIONEIN 1)
Molecular weight formula_weight	4686.6 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	8850

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	1

SOLUTION STRUCTURE OF A ZINC DOMAIN CONSERVED IN YEAST COPPER-REGULATED TRANSCRIPTION FACTORS

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

PROTEIN (ACTIVATOR OF METALLOTHIONEIN 1)

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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

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/co/1co4/1co4.fit
pddf	/app/data/pr_computation/co/1co4/1co4.pr.out
profile	/app/data/saxs_computation/co/1co4/1co4.dat