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- PDB-1chc: STRUCTURE OF THE C3HC4 DOMAIN BY 1H-NUCLEAR MAGNETIC RESONANCE SP... -

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Basic information

Entry
Database: PDB / ID: 1chc
TitleSTRUCTURE OF THE C3HC4 DOMAIN BY 1H-NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; A NEW STRUCTURAL CLASS OF ZINC-FINGER
ComponentsEQUINE HERPES VIRUS-1 RING DOMAIN
KeywordsVIRAL PROTEIN
Function / homology
Function and homology information


symbiont-mediated perturbation of host exit from mitosis / symbiont-mediated disruption of host cell PML body / RING-type E3 ubiquitin transferase / transferase activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity / symbiont-mediated perturbation of host ubiquitin-like protein modification / DNA binding / metal ion binding
Similarity search - Function
Zinc/RING finger domain, C3HC4 (zinc finger) / Herpes Virus-1 / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Ring finger / Zinc finger RING-type profile. / Zinc finger, RING-type / Zinc finger, RING/FYVE/PHD-type / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
E3 ubiquitin-protein ligase ICP0
Similarity search - Component
Biological speciesEquid herpesvirus 1 (Equine herpesvirus 1)
MethodSOLUTION NMR
AuthorsBarlow, P.N. / Everett, R.D. / Luisi, B.
Citation
Journal: J.Mol.Biol. / Year: 1994
Title: Structure of the C3HC4 domain by 1H-nuclear magnetic resonance spectroscopy. A new structural class of zinc-finger.
Authors: Barlow, P.N. / Luisi, B. / Milner, A. / Elliott, M. / Everett, R.
#1: Journal: J.Mol.Biol. / Year: 1993
Title: A Novel Arrangement of Zinc-Binding Residues and Secondary Structure in the C3Hc4 Motif of an Alpha Herpes Virus Protein Family
Authors: Everett, R.D. / Barlow, P. / Milner, A. / Luisi, B. / Orr, A. / Hope, G. / Lyon, D.
#2: Journal: Cell(Cambridge,Mass.) / Year: 1991
Title: A Novel Cysteine-Rich Sequence Motif
Authors: Freemont, P.S. / Handon, I.M. / Trowsdale, J.
History
DepositionFeb 2, 1994Processing site: BNL
Revision 1.0Apr 30, 1994Provider: repository / Type: Initial release
Revision 1.1Mar 3, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_conn_angle / pdbx_struct_oper_list / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: EQUINE HERPES VIRUS-1 RING DOMAIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)7,7833
Polymers7,6521
Non-polymers1312
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Atom site foot note1: CIS PROLINE - PRO 23
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / -
Representative

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Components

#1: Protein EQUINE HERPES VIRUS-1 RING DOMAIN


Mass: 7651.879 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Equid herpesvirus 1 (Equine herpesvirus 1)
Genus: Varicellovirus / References: UniProt: P28990
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

NMR ensembleConformers submitted total number: 1

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