SAXSdb — 9ndt

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

DNA primase

Herpesviridae

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 17–892	Not recorded	DNA replication helicase × 1 （P10189）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.80 Å

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.

Other PDB	Difference from Current Entry 9NDT	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9NDA The rigid portion of Cryo-EM structure of Herpesvirus Helicase-Primase complex with amenamevir Deposited 2025-02-17	Different construct Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 2–1058（1057 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
9NDQ The rigid portion of Cryo-EM structure of Herpesvirus Helicase-Primase complex prepared with forked DNA and ATP-gamma-S Deposited 2025-02-18	Different construct Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 2–1058（1057 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
9NDZ The rigid portion of Cryo-EM structure of Herpesvirus Helicase-Primase complex prepared with forked DNA, ATP-gamma-S and Pritelivir Deposited 2025-02-19	Different construct Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–1058（1058 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
9NE0 The flexible portion of Cryo-EM structure of Herpesvirus Helicase-Primase complex prepared with forked DNA, ATP-gamma-S and Pritelivir Deposited 2025-02-19	Different construct Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 17–1040（1024 aa）	Not recorded	A1BXB Pritelivir × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
9NEB The rigid portion of Cryo-EM structure of Herpesvirus Helicase-Primase complex with Pritelivir Deposited 2025-02-19	Different construct Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–1058（1058 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
9NEE The flexible portion of Cryo-EM structure of Herpesvirus Helicase-Primase complex with Pritelivir Deposited 2025-02-19	Different construct Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–1058（1058 aa）	Not recorded	A1BXB Pritelivir × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
9NEL The flexible portion of Cryo-EM structure of Herpesvirus Helicase-Primase complex with amenamevir Deposited 2025-02-19	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–1058（1058 aa）	Not recorded	A1BXD Amenamevir × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.20 Å
9NN2 Composite structure of HSV-1 helicase-primase in complex with a forked DNA and amenamevir Deposited 2025-03-04	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric	Chain B 1–1058（1058 aa）	Not recorded	A1BXD Amenamevir × 1 ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；CHAPSO is made fresh at 80 mM before being added to the sample at a final concentration of 2 mM immediately before vitrification cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
9NNP Composite structure of HSV-1 helicase-primase in complex with a forked DNA Deposited 2025-03-05	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric	Chain B 1–1058（1058 aa）	Not recorded	ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；CHAPSO is made fresh at 80 mM before being added to the sample at a final concentration of 4 mM immediately before vitrification cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
9NQP Composite structure of HSV1 helicase-primase in complex with a forked DNA and pritelivir Deposited 2025-03-12	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric	Chain B 1–1058（1058 aa）	Not recorded	A1BXB Pritelivir × 1 ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；CHAPSO is made fresh at 80 mM before being added to the sample at a final concentration of 2 mM immediately before vitrification cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
9UT1 The helicase-primase complex from HHV1 bound with ssDNA and amenamevir Deposited 2025-05-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: tetrameric	Chain B 1–1058（1058 aa）	Mutation：R64T/R71E	A1BXD Amenamevir × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.14 Å
9UT3 The helicase module of the helicase-primase complex from HHV1 bound with ssDNA and amenamevir Deposited 2025-05-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: trimeric	Chain B 1–1058（1058 aa）	Mutation：R64T/R71E	A1BXD Amenamevir × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.88 Å
9UT4 The primase module of the helicase-primase complex from HHV1 bound with ssDNA and amenamevir Deposited 2025-05-02	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–1058（1058 aa）	Mutation：R64T/R71E	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.91 Å
9UT5 The helicase-primase complex from HHV1 bound with ssDNA and pritelivir Deposited 2025-05-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: tetrameric	Chain B 1–1058（1058 aa）	Mutation：R64T/R71E	A1BXB Pritelivir × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.32 Å
9UT6 The helicase module of the helicase-primase complex from HHV1 bound with ssDNA and pritelivir Deposited 2025-05-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: trimeric	Chain B 1–1058（1058 aa）	Mutation：R64T/R71E	A1BXB Pritelivir × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.12 Å
9UT7 The Primase module of the helicase-primase complex from HHV1 bound with ssDNA and pritelivir Deposited 2025-05-02	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–1058（1058 aa）	Mutation：R64T/R71E	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.08 Å
9VLQ herpes simplex virus type 1 helicase-primase structure in complex with ssDNA, ADP and magnesium ion Deposited 2025-06-26	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric	Chain C 1–1058（1058 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PRIM_HHV11
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–876； UniProt 17–892

DNA replication helicase

Herpesviridae

UniProt P10189

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 38–882	Not recorded	DNA primase × 1 （P10236）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.80 Å

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.

Other PDB	Difference from Current Entry 9NDT	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9NE0 The flexible portion of Cryo-EM structure of Herpesvirus Helicase-Primase complex prepared with forked DNA, ATP-gamma-S and Pritelivir Deposited 2025-02-19	Different construct Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 36–882（847 aa）	Not recorded	A1BXB Pritelivir × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
9NEE The flexible portion of Cryo-EM structure of Herpesvirus Helicase-Primase complex with Pritelivir Deposited 2025-02-19	Different construct Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 37–882（846 aa）	Not recorded	A1BXB Pritelivir × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
9NEL The flexible portion of Cryo-EM structure of Herpesvirus Helicase-Primase complex with amenamevir Deposited 2025-02-19	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 40–882（843 aa）	Not recorded	A1BXD Amenamevir × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.20 Å
9NN2 Composite structure of HSV-1 helicase-primase in complex with a forked DNA and amenamevir Deposited 2025-03-04	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric	Chain A 31–882（852 aa）	Not recorded	A1BXD Amenamevir × 1 ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；CHAPSO is made fresh at 80 mM before being added to the sample at a final concentration of 2 mM immediately before vitrification cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
9NNP Composite structure of HSV-1 helicase-primase in complex with a forked DNA Deposited 2025-03-05	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric	Chain A 31–882（852 aa）	Not recorded	ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；CHAPSO is made fresh at 80 mM before being added to the sample at a final concentration of 4 mM immediately before vitrification cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
9NQP Composite structure of HSV1 helicase-primase in complex with a forked DNA and pritelivir Deposited 2025-03-12	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric	Chain A 31–882（852 aa）	Not recorded	A1BXB Pritelivir × 1 ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；CHAPSO is made fresh at 80 mM before being added to the sample at a final concentration of 2 mM immediately before vitrification cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
9UT1 The helicase-primase complex from HHV1 bound with ssDNA and amenamevir Deposited 2025-05-02	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: tetrameric	Chain A 1–882（882 aa）	Not recorded	A1BXD Amenamevir × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.14 Å
9UT3 The helicase module of the helicase-primase complex from HHV1 bound with ssDNA and amenamevir Deposited 2025-05-02	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: trimeric	Chain A 1–882（882 aa）	Not recorded	A1BXD Amenamevir × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.88 Å
9UT5 The helicase-primase complex from HHV1 bound with ssDNA and pritelivir Deposited 2025-05-02	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: tetrameric	Chain A 1–882（882 aa）	Not recorded	A1BXB Pritelivir × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.32 Å
9UT6 The helicase module of the helicase-primase complex from HHV1 bound with ssDNA and pritelivir Deposited 2025-05-02	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: trimeric	Chain A 1–882（882 aa）	Not recorded	A1BXB Pritelivir × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.12 Å
9VLQ herpes simplex virus type 1 helicase-primase structure in complex with ssDNA, ADP and magnesium ion Deposited 2025-06-26	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric	Chain A 1–882（882 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	HELI_HHV11
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–845； UniProt 38–882

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	9ndt
Deposition date deposition_date	2025-02-18
Structure title title	The flexible portion of Cryo-EM structure of Herpesvirus Helicase-Primase complex prepared with forked DNA and ATP-gamma-S
Keywords keywords	Helicase, Primase, Forked DNA, REPLICATION, TRANSFERASE; REPLICATION, TRANSFERASE
Experimental Method method	ELECTRON MICROSCOPY

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	29.74 Å
Radius of gyration Rg (electron density) rg_electron	28.95 Å
Forward intensity I(0) i0	74527800.00
Molecular weight molecular_weight	68983.0 kDa
Excluded volume excluded_volume	86913 Å³
Envelope volume envelope_volume	113520 Å³
Hydration-shell volume shell_volume	33082 Å³
Envelope diameter envelope_diameter	101.4 Å
Shell Rg shell_rg	35.78 Å
Envelope Rg envelope_rg	29.14 Å
Shape Rg shape_rg	28.96 Å
Total Rg total_rg	29.62 Å
Total atoms total_atoms	4872
Residues n_residues	616
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	96.0 Å
Rg (real space) rg_real	29.69 Å
Rg uncertainty (real space) rg_real_error	0.67 Å
I(0) (real space) i0_real	7.4530e+07
I(0) uncertainty (real space) i0_real_error	1.1190e+06
Rg (reciprocal space) rg_reciprocal	29.72 Å
I(0) (reciprocal space) i0_reciprocal	74530000.0000
Solution quality estimate total_estimate	0.9034
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	30.8 Å
Skewness Skewness skewness	0.231
Kurtosis Kurtosis kurtosis	-0.599
Angular range angular_range	— – 0.2650 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	22030000.0000
Real-space data points n_real_points	54
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.922; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.983

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	DNA primase
Molecular weight formula_weight	94733.2 kDa
EC 编号 ec_number	2.7.7.-
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	4872

PVEVTALYATDGCVITSSIALLTNSLLGAEPVYIFSYDAYTHDGRADGPTEQDRFEESRALYQASGGLNGDSFRVTFCLLGTEVGGTHQARGRTRPMFVCRFERADDVAALQDALAHGTPLQPDHIAATLDAEATFALHANMILALTVAINNASPRTGRDAAAAQYDQGASLRSLVGRTSLGQRGLTTLYVHHEVRVLAAYRRAYYGSAQSPFWFLSKFGPDEKSLVLTTRYYLLQAQRLGGAGATYDLQAIKDICATYAIPHAPRPDTVSAASLTSFAAITRFCCTSQYARGAAAAGFPLYVERRIAADVRETSALEKFITHDRSCLRVSDREFITYIYLAHFECFSPPRLATHLRAVTTHDPNPAASTEQPSPLGREAVEQFFCHVRAQLNIGEYVKHNVTPRETVLDGDTAKAYLRARTYAPGALTPAPAYCGAVDSATKMMGRLADAEKLLVPRGWPAFAPASPGEDTAGGTPPPQTCGIVKRLLRLAATEQQGPTPPAIAALIRNAAVQTPLPVYRISMVPTGQAFAALAWDDWARITRDARLAEAVVSAEAAAHPDHGALGRRLTDRIRAQGPVMPPGGLDAGGQMYVNRNEIFNGALAITNIILDLDIALKEPVPFRRLHEALGHFRRGALAAVQLLFPAARVDPDAYPCYFFKSACRPGPASVGSGSGLGNDDDGDWFPCYDDAGDEEWAEDPGAMDTSHDPPDDEVAYFDLCHEVGPTAEPRETDSPVCSCTDKIGLRVCMPVPAPYVVHGSLTMRGVARVIQQAVLLDRDFVEAIGSYVKNFLLIDTGVYAHGHSLRLPYFAKIAPDGPACGRLLPVFVIPPACKDVPAFVAAHADPRRFHFHAPPTYLASPREIRVLHSLGGDYV

来源 Source

来源生物 organism	Herpesviridae
NCBI Class编号 ncbi_taxonomy_id	10292
宿主生物 host_organism	Spodoptera frugiperda

Entity 2 Entity 2 polymer

Description description	DNA replication helicase
Molecular weight formula_weight	95015.0 kDa
EC 编号 ec_number	3.6.4.-
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

NFTSMHGVQPILKRIRELSQQQLDGAQVPHLQWFRDVAALESPAGLPLREFPFAVYLITGNAGSGKSTCVQTINEVLDCVVTGATRIAAQNMYAKLSGAFLSRPINTIFHEFGFRGNHVQAQLGQYPYTLTSNPASLEDLQRRDLTYYWEVILDLTKRALAASGGEELRNEFRALAALERTLGLAEGALTRLAPATHGALPAFTRSNVIVIDEAGLLGRHLLTAVVYCWWMINALYHTPQYAARLRPVLVCVGSPTQTASLESTFEHQKLRCSVRQSENVLTYLICNRTLREYARLSYSWAIFINNKRCVEHEFGNLMKVLEYGLPITEEHMQFVDRFVVPENYITNPANLPGWTRLFSSHKEVSAYMAKLHAYLKVTREGEFVVFTLPVLTFVSVKEFDEYRRLTHQPGLTIEKWLTANASRITNYSQSQDQDAGHMRCEVHSKQQLVVARNDVTYVLNSQIAVTARLRKLVFGFSGTFRAFEAVLRDDSFVKTQGETSVEFAYRFLSRLIFSGLISFYNFLQRPGLDATQRTLAYARMGELTAEILSLRPKSSGVPTQASVMADAGAPGERAFDFKQLGPRDGGPDDFPDDDLDVIFAGLDEQQLDVFYCHYTPGEPETTAAVHTQFALLKRAFLGRFRILQELFGEAFEVAPFSTYVDNVIFRGCEMLTGSPRGGLMSVALQTDNYTLMGYTYARVFAFADELRRRHATANVAELLEEAPLPYVVLRDQHGFMSVVNTNISEFVESIDSTELAMAINADYGISSKLAMTITRSQGLSLDKVAICFTPGNLRLNSAYVAMSRTTSSEFLRMNLNPLRERHERDDVISEHILSALRDPNVVIVY

来源 Source

来源生物 organism	Herpesviridae
NCBI Class编号 ncbi_taxonomy_id	10292
宿主生物 host_organism	Spodoptera frugiperda

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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	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	3.80 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	52547

fit	/app/data/saxs_computation/nd/9ndt/9ndt.fit
pddf	/app/data/pr_computation/nd/9ndt/9ndt.pr.out
profile	/app/data/saxs_computation/nd/9ndt/9ndt.dat

The flexible portion of Cryo-EM structure of Herpesvirus Helicase-Primase complex prepared with forked DNA and ATP-gamma-S

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

DNA primase

State in the Current Structure

Other States of the Same Protein in the Database

DNA replication helicase

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)