2voy

CryoEM model of CopA, the copper transporting ATPase from Archaeoglobus fulgidus

Method: ELECTRON MICROSCOPY

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

POTENTIAL COPPER-TRANSPORTING ATPASE

BACILLUS SUBTILIS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 12	SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1 × 1 （P04191） SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1 × 1 （P04191） SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1 × 1 （P04191） SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1 × 1 （P04191） CATION-TRANSPORTING ATPASE, P-TYPE × 1 （O29777） SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1 × 1 （P04191） SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1 × 1 （P04191） CATION-TRANSPORTING ATPASE × 1 CATION-TRANSPORTING ATPASE × 1 （O29777） SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1 × 1 （P04191） SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1 × 1 （P04191）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	COPA_BACSU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–76； UniProt 72–147

SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1

OrganismNot specified

UniProt P04191

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 12	POTENTIAL COPPER-TRANSPORTING ATPASE × 1 （O32220） CATION-TRANSPORTING ATPASE, P-TYPE × 1 （O29777） CATION-TRANSPORTING ATPASE × 1 CATION-TRANSPORTING ATPASE × 1 （O29777）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	AT2A1_RABIT
Isoform	—
PDB entities	2, 3, 4, 5, 7, 8, 11, 12
Chains and sequence ranges	Author chain B； PDBConstruct 1–42； UniProt 36–77 Author chain C； PDBConstruct 1–22； UniProt 967–988 Author chain D； PDBConstruct 1–23； UniProt 832–854 Author chain E； PDBConstruct 1–30； UniProt 86–115 Author chain G； PDBConstruct 1–36； UniProt 243–278 Author chain H； PDBConstruct 1–48； UniProt 289–336 Author chain K； PDBConstruct 1–32； UniProt 749–780 Author chain L； PDBConstruct 1–21； UniProt 789–809

CATION-TRANSPORTING ATPASE, P-TYPE

ARCHAEOGLOBUS FULGIDUS

UniProt O29777

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 12	POTENTIAL COPPER-TRANSPORTING ATPASE × 1 （O32220） SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1 × 1 （P04191） SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1 × 1 （P04191） SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1 × 1 （P04191） SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1 × 1 （P04191） SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1 × 1 （P04191） SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1 × 1 （P04191） CATION-TRANSPORTING ATPASE × 1 SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1 × 1 （P04191） SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1 × 1 （P04191）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	O29777_ARCFU
Isoform	—
PDB entities	6, 10
Chains and sequence ranges	Author chain F； PDBConstruct 1–113； UniProt 214–326 Author chain J； PDBConstruct 1–118； UniProt 432–549

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	2voy
Deposition date deposition_date	2008-02-25
Structure title title	CryoEM model of CopA, the copper transporting ATPase from Archaeoglobus fulgidus
Keywords keywords	HYDROLASEP-TYPE ATPASE, CRYO-EM, HELICAL RECONSTRUCTION, MEMBRANE PROTEIN, COPPER TRANSPORTER, METAL BINDING DOMAIN, HYDROLASE; HYDROLASE
Experimental Method method	ELECTRON MICROSCOPY

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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.

2voy__assembly_1__model_1

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

Download this curve (.dat)

2voy__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2voy__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	32.75 Å
Rg (electron density)	33.53 Å
Total Rg	33.76 Å
Atom count	5270
Residues	690
Excluded volume	95566 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2voy__assembly_1__model_1`	dodecameric （12）	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 (12)

Entity 1 Entity 1 polymer

Description description	POTENTIAL COPPER-TRANSPORTING ATPASE
Molecular weight formula_weight	8800.0 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	A
Atom count atom_count	5270

VTEKAEFDIEGMTCAACANRIEKRLNKIEGVANAPVNFALETVTVEYNPKEASVSDLKEAVDKLGYKLKLKGEQDSIEGR

Source Source

Source organism organism	BACILLUS SUBTILIS
NCBI taxonomy ID ncbi_taxonomy_id	1423
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1
Molecular weight formula_weight	4832.6 kDa
EC 编号 ec_number	3.6.3.8
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

YGHNELPAEEGKSLWELVIEQFEDLLVRILLLAACISFVLAW

Entity 3 Entity 3 polymer

Description description	SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1
Molecular weight formula_weight	2514.2 kDa
EC 编号 ec_number	3.6.3.8
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

WLMVLKISLPVIGLDEILKFIA

Entity 4 Entity 4 polymer

Description description	SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1
Molecular weight formula_weight	2479.9 kDa
EC 编号 ec_number	3.6.3.8
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D

WLFFRYMAIGGYVGAATVGAAAW

Entity 5 Entity 5 polymer

Description description	SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1
Molecular weight formula_weight	3312.8 kDa
EC 编号 ec_number	3.6.3.8
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E

TAFVEPFVILLILIANAIVGVWQERNAENA

Entity 6 Entity 6 polymer

Description description	CATION-TRANSPORTING ATPASE, P-TYPE
Molecular weight formula_weight	11832.7 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	F

EAIKKLVGLQAKTAVVIRDGKEIAVPVEEVAVGDIVIVRPGEKIPVDGVVVEGESYVDESMISGEPVPVLKSKGDEVFGATINNTGVLKIRATRVGGETLLAQIVKLVEDAMG

Source Source

Source organism organism	ARCHAEOGLOBUS FULGIDUS
NCBI taxonomy ID ncbi_taxonomy_id	2234
Host organism host_organism	ESCHERICHIA COLI

Entity 7 Entity 7 polymer

Description description	SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1
Molecular weight formula_weight	4097.7 kDa
EC 编号 ec_number	3.6.3.8
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G

EQDKTPLQQKLDEFGEQLSKVISLICVAVWLINIGH

Entity 8 Entity 8 polymer

Description description	SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1
Molecular weight formula_weight	5093.2 kDa
EC 编号 ec_number	3.6.3.8
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H

IRGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSL

Entity 9 Entity 9 polymer

Description description	CATION-TRANSPORTING ATPASE
Molecular weight formula_weight	13783.5 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	I

DALEVAEKVTAVIFDKTGTLTKLKESAKPAVQELKRMGIKVGMITGDNWRSAEAISRELNLDLVIAEVLPHQKSEEVKKLQAKEVVAFVGDGINDAPALAQADLGIAVGSGDIVLIRDDLRDVVAAIQ

Source Source

Source organism organism	ARCHAEOGLOBUS FULGIDUS
NCBI taxonomy ID ncbi_taxonomy_id	2234
Host organism host_organism	ESCHERICHIA COLI

Entity 10 Entity 10 polymer

Description description	CATION-TRANSPORTING ATPASE
Molecular weight formula_weight	12705.3 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	J

GKPEVTDLVPLNGDERELLRLAAIAERRSEHPIAEAIVKKALEHGIELGEPEKVEVIAGEGVVADGILVGNKRLMEDFGVAVSNEVELALEKLEREAKTAVIVARNGRVEGIIAVSDT

Source Source

Source organism organism	ARCHAEOGLOBUS FULGIDUS
NCBI taxonomy ID ncbi_taxonomy_id	2234
Host organism host_organism	ESCHERICHIA COLI

Entity 11 Entity 11 polymer

Description description	SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1
Molecular weight formula_weight	3624.2 kDa
EC 编号 ec_number	3.6.3.8
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	K

EGRAIYNNMKQFIRYLISSNVGEVVCIFLTAA

Entity 12 Entity 12 polymer

Description description	SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1
Molecular weight formula_weight	2224.6 kDa
EC 编号 ec_number	3.6.3.8
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	L

PVQLLWVNLVTDGLPATALGF

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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	—

Resolution resolution	18.00 Å
Resolution测定Method resolution_method	;TUBES DIVIDED INTO THIRDS, QUARTERS, OR FIFTHS AND CORRECTED FOR IN-PLACE ROTATION, OUT-OF-PLANE TILT, Z-SHIFT, ROTATION ABOUT Z-AXIS ;
颗粒数 num_particles	—

CryoEM model of CopA, the copper transporting ATPase from Archaeoglobus fulgidus

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

POTENTIAL COPPER-TRANSPORTING ATPASE

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

CATION-TRANSPORTING ATPASE, P-TYPE

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

2voy__assembly_1__model_1

2voy__assembly_1__model_1 | I(q)

2voy__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (12)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

Entity 5 Entity 5 polymer

Polymer Polymer

Entity 6 Entity 6 polymer

Polymer Polymer

Source Source

Entity 7 Entity 7 polymer

Polymer Polymer

Entity 8 Entity 8 polymer

Polymer Polymer

Entity 9 Entity 9 polymer

Polymer Polymer

Source Source

Entity 10 Entity 10 polymer

Polymer Polymer

Source Source

Entity 11 Entity 11 polymer

Polymer Polymer

Entity 12 Entity 12 polymer

Polymer Polymer

7. Citations (1)