SAXSdb — 9ycv

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

UL52

Human alphaherpesvirus 1 strain R-15

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–DNA Heteromer Protein × 3 DNA 1 PDB declaration: tetrameric（4） Consistent with all polymer counts	Chain C； UniProt 1–1058	Not recorded	;DNA (5'-D(TPTPTPTPTPT)-3') ; × 1 UL5 × 1 （A0A5J6DVR7） UL8 × 1 （P10192） ZN ZINC ION × 1 A1BXD Amenamevir × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.80 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 9YCV	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9YC9 HSV replication fork complex bound to pritelivir Deposited 2025-09-18	Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 5 PDB declaration: octameric	Chain C 1–1058（1058 aa）	Not recorded	ZN ZINC ION × 1 A1BXB Pritelivir × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
9YCP HSV Helicase-primase complex bound to IM-250 Deposited 2025-09-19	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	ZN ZINC ION × 1 A1CHB N-{5-[(R)-amino(hydroxy)(methyl)-lambda~4~-sulfanyl]-4-methyl-1,3-thiazol-2-yl}-2-(2',5'-difluoro[1,1'-biphenyl]-4-yl)-N-methylacetamide × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
9YCT HSV helicase-primase complex bound to pritelivir Deposited 2025-09-19	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	ZN ZINC ION × 1 A1BXB Pritelivir × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A5J6DWG4_HHV1
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–1058； UniProt 1–1058

UL5

Human alphaherpesvirus 1 strain R-15

UniProt A0A5J6DVR7

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–DNA Heteromer Protein × 3 DNA 1 PDB declaration: tetrameric（4） Consistent with all polymer counts	Chain A； UniProt 1–882	Not recorded	;DNA (5'-D(TPTPTPTPTPT)-3') ; × 1 UL52 × 1 （A0A5J6DWG4） UL8 × 1 （P10192） ZN ZINC ION × 1 A1BXD Amenamevir × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.80 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 9YCV	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9YC9 HSV replication fork complex bound to pritelivir Deposited 2025-09-18	Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 5 PDB declaration: octameric	Chain A 1–882（882 aa）	Not recorded	ZN ZINC ION × 1 A1BXB Pritelivir × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
9YCP HSV Helicase-primase complex bound to IM-250 Deposited 2025-09-19	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	ZN ZINC ION × 1 A1CHB N-{5-[(R)-amino(hydroxy)(methyl)-lambda~4~-sulfanyl]-4-methyl-1,3-thiazol-2-yl}-2-(2',5'-difluoro[1,1'-biphenyl]-4-yl)-N-methylacetamide × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
9YCT HSV helicase-primase complex bound to pritelivir Deposited 2025-09-19	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	ZN ZINC ION × 1 A1BXB Pritelivir × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A5J6DVR7_HHV1
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain A； PDBConstruct 1–882； UniProt 1–882

UL8

Human alphaherpesvirus 1 strain R-15

UniProt P10192

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–DNA Heteromer Protein × 3 DNA 1 PDB declaration: tetrameric（4） Consistent with all polymer counts	Chain B； UniProt 1–750	Not recorded	;DNA (5'-D(TPTPTPTPTPT)-3') ; × 1 UL52 × 1 （A0A5J6DWG4） UL5 × 1 （A0A5J6DVR7） ZN ZINC ION × 1 A1BXD Amenamevir × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.80 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 9YCV	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 oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–750（750 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 oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–750（750 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 oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–750（750 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
9NEB The rigid portion of Cryo-EM structure of Herpesvirus Helicase-Primase complex with Pritelivir Deposited 2025-02-19	Different oligomeric state Different ligand/ion	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–750（750 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
9NN2 Composite structure of HSV-1 helicase-primase in complex with a forked DNA and amenamevir Deposited 2025-03-04	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric	Chain C 1–750（750 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 ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric	Chain C 1–750（750 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 ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric	Chain C 1–750（750 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 mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: tetrameric	Chain C 1–750（750 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
9UT4 The primase module of the helicase-primase complex from HHV1 bound with ssDNA and amenamevir Deposited 2025-05-02	Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–750（750 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 mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: tetrameric	Chain C 1–750（750 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
9UT7 The Primase module of the helicase-primase complex from HHV1 bound with ssDNA and pritelivir Deposited 2025-05-02	Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–750（750 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
9YC9 HSV replication fork complex bound to pritelivir Deposited 2025-09-18	Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 5 PDB declaration: octameric	Chain B 1–750（750 aa）	Not recorded	ZN ZINC ION × 1 A1BXB Pritelivir × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
9YCP HSV Helicase-primase complex bound to IM-250 Deposited 2025-09-19	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric	Chain B 1–750（750 aa）	Not recorded	ZN ZINC ION × 1 A1CHB N-{5-[(R)-amino(hydroxy)(methyl)-lambda~4~-sulfanyl]-4-methyl-1,3-thiazol-2-yl}-2-(2',5'-difluoro[1,1'-biphenyl]-4-yl)-N-methylacetamide × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
9YCT HSV helicase-primase complex bound to pritelivir Deposited 2025-09-19	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric	Chain B 1–750（750 aa）	Not recorded	ZN ZINC ION × 1 A1BXB Pritelivir × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	HEPA_HHV11
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain B； PDBConstruct 1–750； UniProt 1–750

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	9ycv
Deposition date deposition_date	2025-09-19
Structure title title	HSV Helicase-primase complex bound to amenamevir
Keywords keywords	HSV, helicase-primase, HPI, VIRAL PROTEIN; VIRAL PROTEIN
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	53.32 Å
Radius of gyration Rg (electron density) rg_electron	53.65 Å
Forward intensity I(0) i0	1710160000.00
Molecular weight molecular_weight	228040.0 kDa
Excluded volume excluded_volume	220340 Å³
Envelope volume envelope_volume	449570 Å³
Hydration-shell volume shell_volume	73570 Å³
Envelope diameter envelope_diameter	193.0 Å
Shell Rg shell_rg	52.26 Å
Envelope Rg envelope_rg	52.65 Å
Shape Rg shape_rg	53.65 Å
Total Rg total_rg	53.61 Å
Total atoms total_atoms	17325
Residues n_residues	2222
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	187.4 Å
Rg (real space) rg_real	53.65 Å
Rg uncertainty (real space) rg_real_error	2.00 Å
I(0) (real space) i0_real	1.7100e+09
I(0) uncertainty (real space) i0_real_error	3.3110e+07
Rg (reciprocal space) rg_reciprocal	53.03 Å
I(0) (reciprocal space) i0_reciprocal	1709000000.0000
Solution quality estimate total_estimate	0.8389
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	50.0 Å
Skewness Skewness skewness	0.477
Kurtosis Kurtosis kurtosis	-0.452
Angular range angular_range	— – 0.1500 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	52020000.0000
Real-space data points n_real_points	31
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.752; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.947; Smooth: 0.699

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	;DNA (5'-D(TPTPTPTPTPT)-3') ;
Molecular weight formula_weight	1780.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polydeoxyribonucleotide
Chain IDs strand_id	D
Atom count atom_count	17325

TTTTTT

来源 Source

来源生物 organism	Human alphaherpesvirus 1 strain R-15
NCBI Class编号 ncbi_taxonomy_id	36345
宿主生物 host_organism	Homo sapiens

Entity 2 Entity 2 polymer

Description description	UL52
Molecular weight formula_weight	114558.6 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

MGQEDGNRGERRAAGTPVEVTALYATDGCVITSSIALLTNSLLGAEPVYIFSYDAYTHDGRADGPTEQDRFEESRALYQASGGLNGDSFRVTFCLLGTEVGGTHQARGRTRPMFVCRFERADDVAALQDALAHGTPLQPDHIAATLDAEATFALHANMILALTVAINNASPRTGRDAAAAQYDQGASLRSLVGRTSLGQRGLTTLYVHHEVRVLAAYRRAYYGSAQSPFWFLSKFGPDEKSLVLTTRYYLLQAQRLGGAGATYDLQAIKDICATYAIPHAPRPDTVSAASLTSFAAITRFCCTSQYARGAAAAGFPLYVERRIAADVRETSALEKFITHDRSCLRVSDREFITYIYLAHFECFSPPRLATHLRAVTTHDPNPAASTEQPSPLGREAVEQFFCHVRAQLNIGEYVKHNVTPRETVLDGDTAKAYLRARTYAPGALTPAPAYCGAVDSATKMMGRLADAEKLLVPRGWPAFAPASPGEDTAGGTPPPQTCGIVKRLLRLAATEQQGPTPPAIAALIRNAAVQTPLPVYRISMVPTGQAFAALAWDDWARITRDARLAEAVVSAEAAAHPDHGALGRRLTDRIRAQGPVMPPGGLDAGGQMYVNRNEIFNGALAITNIILDLDIALKEPVPFRRLHEALGHFRRGALAAVQLLFPAARVDPDAYPCYFFKSACRPGPASVGSGSGLGNDDDGDWFPCYDDAGDEEWAEDPGAMDTSHDPPDDEVAYFDLCHEVGPTAEPRETDSPVCSCTDKIGLRVCMPVPAPYVVHGSLTMRGVARVIQQAVLLDRDFVEAIGSYVKNFLLIDTGVYAHGHSLRLPYFAKIAPDGPACGRLLPVFVIPPACKDVPAFVAAHADPRRFHFHAPPTYLASPREIRVLHSLGGDYVSFFERKASRNALEHFGRRETLTEVLGRYNVQPDAGGTVEGFASELLGRIVACIETHFPEHAGEYQAVSVRRAVSKDDWVLLQLVPVRGTLQQSLSCLRFKHGRASRATARTFVALSVGANNRLCVSLCQQCFAAKCDSNRLHTLFTIDAGTPCSPSVPCSTSQPSS

来源 Source

来源生物 organism	Human alphaherpesvirus 1 strain R-15
NCBI Class编号 ncbi_taxonomy_id	36345
宿主生物 host_organism	Homo sapiens

Entity 3 Entity 3 polymer

Description description	UL5
Molecular weight formula_weight	98823.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A

MAAAGGERQLDGQKPGPPHLQQPGDRPAVPGRAEAFLNFTSMHGVQPILKRIRELSQQQLDGAQVPHLQWFRDVAALESPAGLPLREFPFAVYLITGNAGSGKSTCVQTINEVLDCVVTGATRIAAQNMYAKLSGAFLSRPINTIFHEFGFRGNHVQAQLGQYPYTLTSNPASLEDLQRRDLTYYWEVILDLTKRALAASGGEELRNEFRALAALERTLGLAEGALTRLAPATHGALPAFTRSNVIVIDEAGLLGRHLLTAVVYCWWMINALYHTPQYAARLRPVLVCVGSPTQTASLESTFEHQKLRCSVRQSENVLTYLICNRTLREYARLSYSWAIFINNKRCVEHEFGNLMKVLEYGLPITEEHMQFVDRFVVPENYITNPANLPGWTRLFSSHKEVSAYMAKLHAYLKVTREGEFVVFTLPVLTFVSVKEFDEYRRLTHQPGLTIEKWLTANASRITNYSQSQDQDAGHMRCEVHSKQQLVVARNDVTYVLNSQIAVTARLRKLVFGFSGTFRAFEAVLRDDSFVKTQGETSVEFAYRFLSRLIFSGLISFYNFLQRPGLDATQRTLAYARMGELTAEILSLRPKSSGVPTQASVMADAGAPGERAFDFKQLGPRDGGPDDFPDDDLDVIFAGLDEQQLDVFYCHYTPGEPETTAAVHTQFALLKRAFLGRFRILQELFGEAFEVAPFSTYVDNVIFRGCEMLTGSPRGGLMSVALQTDNYTLMGYTYARVFAFADELRRRHATANVAELLEEAPLPYVVLRDQHGFMSVVNTNISEFVESIDSTELAMAINADYGISSKLAMTITRSQGLSLDKVAICFTPGNLRLNSAYVAMSRTTSSEFLRMNLNPLRERHERDDVISEHILSALRDPNVVIVY

来源 Source

来源生物 organism	Human alphaherpesvirus 1 strain R-15
NCBI Class编号 ncbi_taxonomy_id	36345
宿主生物 host_organism	Homo sapiens

Entity 4 Entity 4 polymer

Description description	UL8
Molecular weight formula_weight	80005.7 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

MDTADIVWVEESVSAITLYAVWLPPRAREYFHALVYFVCRNAAGEGRARFAEVSVTATELRDFYGSADVSVQAVVAAARAATTPAASPLEPLENPTLWRALYACVLAALERQTGPVALFAPLRIGSDPRTGLVVKVERASWGPPAAPRAALLVAEANIDIDPMALAARVAEHPDARLAWARLAAIRDTPQCASAASLTVNITTGTALFAREYQTLAFPPIKKEGAFGDLVEVCEVGLRPRGHPQRVTARVLLPRDYDYFVSAGEKFSAPALVALFRQWHTTVHAAPGALAPVFAFLGPEFEVRGGPVPYFAVLGFPGWPTFTVPATAESARDLVRGAAAAYAALLGAWPAVGARVVLPPRAWPGVASAAAGCLLPAVREAVARWHPATKIIQLLDPPAAVGPVWTARFCFPGLRAQLLAALADLGGSGLADPHGRTGLARLDALVVAAPSEPWAGAVLERLVPDTCNACPALRQLLGGVMAAVCLQIEETASSVKFAVCGGDGGAFWGVFNVDPQDADAASGVIEDARRAIETAVGAVLRANAVRLRHPLCLALEGVYTHAVAWSQAGVWFWNSRDNTDHLGGFPLRGPAYTTAAGVVRDTLRRVLGLTTACVPEEDALTARGLMEDACDRLILDAFNKRLDAEYWSVRVSPFEASDPLPPTAFRGGALLDAEHYWRRVVRVCPGGGESVGVPVDLYPRPLVLPPVDCAHHLREILREIELVFTGVLAGVWGEGGKFVYPFDDKMSFLFA

来源 Source

来源生物 organism	Human alphaherpesvirus 1 strain R-15
NCBI Class编号 ncbi_taxonomy_id	36345
宿主生物 host_organism	Homo sapiens

Entity 5 Entity 5 non-polymer

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

Entity 6 Entity 6 non-polymer

Description description	Amenamevir
Molecular weight formula_weight	482.6 kDa
Source method src_method	syn
Copy count entity_count	1

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8. Citations (1)

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Resolution resolution	2.80 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	340000

fit	/app/data/saxs_computation/yc/9ycv/9ycv.fit
pddf	/app/data/pr_computation/yc/9ycv/9ycv.pr.out
profile	/app/data/saxs_computation/yc/9ycv/9ycv.dat

HSV Helicase-primase complex bound to amenamevir

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

UL52

State in the Current Structure

Other States of the Same Protein in the Database

UL5

State in the Current Structure

Other States of the Same Protein in the Database

UL8

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 polymer

Polymer Polymer

来源 Source

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)