7apd

Bovine Papillomavirus E1 DNA helicase-replication fork complex

Method: ELECTRON MICROSCOPY

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

Replication protein E1

Bovine papillomavirus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–DNA	Heteromer	Protein 8 DNA 2	Replication protein E1 × 6 （P03116） DNA (40-MER) × 1 DNA (36-MER) × 1	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	C5IAS0_9PAPI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain G； PDBConstruct 4–148； UniProt 159–303 Author chain H； PDBConstruct 4–148； UniProt 159–303

Replication protein E1

Bovine papillomavirus

UniProt P03116

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–DNA	Heteromer	Protein 8 DNA 2	Replication protein E1 × 2 （C5IAS0） DNA (40-MER) × 1 DNA (36-MER) × 1	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	VE1_BPV1
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain A； PDBConstruct 1–298； UniProt 308–605 Author chain B； PDBConstruct 1–298； UniProt 308–605 Author chain C； PDBConstruct 1–298； UniProt 308–605 Author chain D； PDBConstruct 1–298； UniProt 308–605 Author chain E； PDBConstruct 1–298； UniProt 308–605 Author chain F； PDBConstruct 1–298； UniProt 308–605

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	7apd
Deposition date deposition_date	2020-10-16
Structure title title	Bovine Papillomavirus E1 DNA helicase-replication fork complex
Keywords keywords	DNA, virus, helicase, replisome, DNA replication., DNA BINDING PROTEIN; DNA BINDING PROTEIN
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.

7apd__assembly_1__model_1

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

Download this curve (.dat)

7apd__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

7apd__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	46.54 Å
Rg (electron density)	45.84 Å
Total Rg	46.25 Å
Atom count	17296
Residues	2096
Excluded volume	303160 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`7apd__assembly_1__model_1`	decameric （10）	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 (4)

Entity 1 Entity 1 polymer

Description description	Replication protein E1
Molecular weight formula_weight	17162.1 kDa
EC 编号 ec_number	3.6.4.12
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G,H
Atom count atom_count	17296

GSRATVFKLGLFKSLFLCSFHDITRLFKNDKTTNQQWVLAVFGLAEVFFEASFELLKKQCSFLQMQKRSHEGGTCAVYLICFNTAKSRETVRNLMANMLNVREECLMLQPPKIRGLSAALFWFKSSLSPATLKHGALPEWIRAQTTLNAAAA

Source Source

Source organism organism	Bovine papillomavirus
NCBI taxonomy ID ncbi_taxonomy_id	10571
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Replication protein E1
Molecular weight formula_weight	33859.2 kDa
EC 编号 ec_number	3.6.4.12
Source method src_method	man
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,C,D,E,F,A

TEKFDFGTMVQWAYDHKYAEESKIAYEYALAAGSDSNARAFLATNSQAKHVKDCATMVRHYLRAETQALSMPAYIKARCKLATGEGSWKSILTFFNYQNIELITFINALKLWLKGIPKKNCLAFIGPPNTGKSMLCNSLIHFLGGSVLSFANHKSHFWLASLADTRAALVDDATHACWRYFDTYLRNALDGYPVSIDRKHKAAVQIKAPPLLVTSNIDVQAEDRYLYLHSRVQTFRFEQPCTDESGEQPFNITDADWKSFFVRLWGRLDLIDEEEDSEEDGDSMRTFTCSARNTNAVD

Source Source

Source organism organism	Bovine papillomavirus
NCBI taxonomy ID ncbi_taxonomy_id	10571
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	DNA (40-MER)
Molecular weight formula_weight	12142.8 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polydeoxyribonucleotide
Chain IDs strand_id	P

TGTATTTCACACCGCACCTCAGCGCGTTTTTTTTTTTTTT

Entity 4 Entity 4 polymer

Description description	DNA (36-MER)
Molecular weight formula_weight	11080.1 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polydeoxyribonucleotide
Chain IDs strand_id	T

CCCCCCCGTGCGCGCTGAGGTGCGGTGTGAAATACA

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6. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id	7apdA01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily	510 — Zinc finger, large T-antigen D1 domain

Domain ID domain_id	7apdA02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	7apdB01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily	510 — Zinc finger, large T-antigen D1 domain

Domain ID domain_id	7apdB02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	7apdC01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily	510 — Zinc finger, large T-antigen D1 domain

Domain ID domain_id	7apdC02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	7apdD01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily	510 — Zinc finger, large T-antigen D1 domain

Domain ID domain_id	7apdD02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	7apdE01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily	510 — Zinc finger, large T-antigen D1 domain

Domain ID domain_id	7apdE02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	7apdF01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily	510 — Zinc finger, large T-antigen D1 domain

Domain ID domain_id	7apdF02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

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Resolution resolution	3.90 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	81831

Bovine Papillomavirus E1 DNA helicase-replication fork complex

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

Replication protein E1

State in the Current Structure

Other States of the Same Protein in the Database

Replication protein E1

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

7apd__assembly_1__model_1

7apd__assembly_1__model_1 | I(q)

7apd__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

6. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

7. Citations (1)

Bovine Papillomavirus E1 DNA helicase-replication fork complex

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

Replication protein E1

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Replication protein E1

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

7apd__assembly_1__model_1

7apd__assembly_1__model_1 | I(q)

7apd__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

6. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

7. Citations (1)