SAXSdb — 2zmy

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

Tyrosinase

STREPTOMYCES CASTANEOGLOBISPORUS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	CADDIE × 1 COPPER (II) ION × 5 NITRATE ION × 6 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q83WS2_9ACTO
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–273； UniProt 1–273

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	2zmy
Deposition date deposition_date	2008-04-21
Structure title title	Crystal structure of the met2-form of the copper-bound tyrosinase in complex with a caddie protein from Streptomyces castaneoglobisporus obtained by soaking in cupric sulfate solution for 80 hours
Keywords keywords	TYROSINASE, BINARY COMPLEX, TYPE-3 COPPER, DIOXYGEN, COPPER TRANSFER, OXIDOREDUCTASE-METAL TRANSPORT COMPLEX, Copper, Metal-binding; OXIDOREDUCTASE/METAL TRANSPORT
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

2zmy__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2zmy__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2zmy__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	20.58 Å
Rg (electron density)	19.47 Å
Total Rg	20.40 Å
Atom count	2860
Residues	355
Excluded volume	49659 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2zmy__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Tyrosinase
Molecular weight formula_weight	32089.6 kDa
EC 编号 ec_number	1.14.18.1
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	3269

MTVRKNQATLTADEKRRFVAAVLELKRSGRYDEFVRTHNEFIMSDTDSGERTGHRSPSFLPWHRRFLLDFEQALQSVDSSVTLPYWDWSADRTVRASLWAPDFLGGTGRSTDGRVMDGPFAASTGNWPINVRVDSRTYLRRSLGGSVAELPTRAEVESVLAISAYDLPPYNSASEGFRNHLEGWRGVNLHNRVHVWVGGQMATGVSPNDPVFWLHHAYVDKLWAEWQRRHPDSAYVPTGGTPDVVDLNETMKPWNTVRPADLLDHTAYYTFDALEHHHHHH

Source Source

Source organism organism	STREPTOMYCES CASTANEOGLOBISPORUS
NCBI taxonomy ID ncbi_taxonomy_id	79261
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	CADDIE
Molecular weight formula_weight	14203.8 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

MPEITRRRALTAAAAVAATASAAVTLAAPAASAAGHHEPAAPESFDEVYKGRRIQGRPARGAAHHHEHGGGYEVFVDGVQLHVMRNADGSWISVVSHYDPVPTPRAAARAAVDELQGAPLLPFPANLEHHHHHH

Source Source

Source organism organism	STREPTOMYCES CASTANEOGLOBISPORUS
NCBI taxonomy ID ncbi_taxonomy_id	79261
Host organism host_organism	ESCHERICHIA COLI

Entity 3 Entity 3 non-polymer

Description description	COPPER (II) ION
Molecular weight formula_weight	63.5 kDa
Source method src_method	syn
Copy count entity_count	5

Entity 4 Entity 4 non-polymer

Description description	NITRATE ION
Molecular weight formula_weight	62.0 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	384

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6. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d2zmya1
Class class	a — All alpha proteins
Fold Fold fold	a.86 — Di-copper centre-containing domain
Superfamily Superfamily superfamily	a.86.1 — Di-copper centre-containing domain
Family Family family	a.86.1.3 — Tyrosinase

Domain ID domain_id	d2zmya2
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

Domain ID domain_id	d2zmyb_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.386 — Tyrosinase cofactor MelC1-like
Superfamily Superfamily superfamily	d.386.1 — Tyrosinase cofactor MelC1
Family Family family	d.386.1.1 — Tyrosinase cofactor MelC1

CATH v4.4 (2 domains)

Domain ID domain_id	2zmyA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1280 — di-copper center containing domain from catechol oxidase
Homologous superfamily homologous superfamily	10 — Di-copper center containing domain from catechol oxidase

Domain ID domain_id	2zmyB01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1880 — protein ne1242 fold
Homologous superfamily homologous superfamily	10 — protein ne1242 domain like

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Unit-cell length a length_a	64.740 Å
Unit-cell length b length_b	97.550 Å
Unit-cell length c length_c	54.970 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	4

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	1.450 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.1690
R_work r_work	0.1686
R_free r_free	0.2137

Crystal structure of the met2-form of the copper-bound tyrosinase in complex with a caddie protein from Streptomyces castaneoglobisporus obtained by soaking in cupric sulfate solution for 80 hours

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

Tyrosinase

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

2zmy__assembly_1__model_1

2zmy__assembly_1__model_1 | I(q)

2zmy__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

CATH v4.4 (2 domains)

7. Citations (2)

Crystal structure of the met2-form of the copper-bound tyrosinase in complex with a caddie protein from Streptomyces castaneoglobisporus obtained by soaking in cupric sulfate solution for 80 hours

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

Tyrosinase

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

2zmy__assembly_1__model_1

2zmy__assembly_1__model_1 | I(q)

2zmy__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

CATH v4.4 (2 domains)

7. Citations (2)