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(-) Description

Title :  THE CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF MU PHAGE CENTRAL SPIKE - PT DERIVATIVE FOR MAD
 
Authors :  K. Harada, E. Yamashita, A. Nakagawa, S. Takeda
Date :  01 Jun 12  (Deposition) - 06 Feb 13  (Release) - 06 Feb 13  (Revision)
Method :  X-RAY DIFFRACTION
Resolution :  1.75
Chains :  Asym. Unit :  A
Biol. Unit 1:  A  (3x)
Keywords :  Beta-Helix, Central Spike, Mu Phage, Metal Binding Protein (Keyword Search: [Gene Ontology, PubMed, Web (Google)] )
 
Reference :  K. Harada, E. Yamashita, A. Nakagawa, T. Miyafusa, K. Tsumoto, T. Ueno Y. Toyama, S. Takeda
Crystal Structure Of The C-Terminal Domain Of Mu Phage Central Spike And Functions Of Bound Calcium Ion
Biochim. Biophys. Acta V. 1834 284 2013
PubMed-ID: 22922659  |  Reference-DOI: 10.1016/J.BBAPAP.2012.08.015

(-) Compounds

Molecule 1 - PROTEIN GP45
    Chains: A
    Engineered: YES
    Expression System: ESCHERICHIA COLI
    Expression System Taxid: 562
    Expression System Vector Type: PLASMID
    Fragment: UNP RESIDUES 100-197
    Gene: 45
    Organism Scientific: ENTEROBACTERIA PHAGE MU
    Organism Taxid: 10677

 Structural Features

(-) Chains, Units

  1
Asymmetric Unit : A
Biological Unit 1 (3x): A

Summary Information (see also Sequences/Alignments below)

(-) Ligands, Modified Residues, Ions  (2, 2)

Asymmetric Unit (2, 2)
No.NameCountTypeFull Name
1FE1Ligand/IonFE (III) ION
2PT1Ligand/IonPLATINUM (II) ION
Biological Unit 1 (0, 0)
No.NameCountTypeFull Name
1FE-1Ligand/IonFE (III) ION
2PT-1Ligand/IonPLATINUM (II) ION

(-) Sites  (1, 1)

Asymmetric Unit (1, 1)
No.NameEvidenceResiduesDescription
1AC1SOFTWAREHIS A:183BINDING SITE FOR RESIDUE FE A 202

(-) SS Bonds  (0, 0)

(no "SS Bond" information available for 3VTN)

(-) Cis Peptide Bonds  (0, 0)

(no "Cis Peptide Bond" information available for 3VTN)

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

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(-) PROSITE Motifs  (0, 0)

(no "PROSITE Motif" information available for 3VTN)

(-) Exons   (0, 0)

(no "Exon" information available for 3VTN)

(-) Sequences/Alignments

Asymmetric Unit
   Reformat: Number of residues per line =  ('0' or empty: single-line sequence representation)
  Number of residues per labelling interval =   
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SAPs(SNPs) PROSITE motifs Exons
(details for a mapped element are shown in a popup box when the mouse pointer rests over it) 
Chain A from PDB  Type:PROTEIN  Length:71
 aligned with BP45_BPMU | Q9T1V4 from UniProtKB/Swiss-Prot  Length:197

    Alignment length:71
                                   122       132       142       152       162       172       182 
            BP45_BPMU   113 RIRLTKDGRCIITCKTVEVYADESMTVDTPRTTFTGDVEIQKGLGVKGKSQFDSNITAPDAIINGKSTDKH 183
               SCOP domains ----------------------------------------------------------------------- SCOP domains
               CATH domains ----------------------------------------------------------------------- CATH domains
               Pfam domains ----------------------------------------------------------------------- Pfam domains
         Sec.struct. author .eee.....eee.................................................hhhhh..... Sec.struct. author
                 SAPs(SNPs) ----------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE ----------------------------------------------------------------------- PROSITE
                 Transcript ----------------------------------------------------------------------- Transcript
                 3vtn A 113 RIRLTKDGRCIITCKTVEVYADESMTVDTPRTTFTGDVEIQKGLGVKGKSQFDSNITAPDAIINGKSTDKH 183
                                   122       132       142       152       162       172       182
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 Classification and Annotation

(-) SCOP Domains  (0, 0)

(no "SCOP Domain" information available for 3VTN)

(-) CATH Domains  (0, 0)

(no "CATH Domain" information available for 3VTN)

(-) Pfam Domains  (0, 0)

(no "Pfam Domain" information available for 3VTN)

(-) Gene Ontology  (5, 5)

Asymmetric Unit(hide GO term definitions)
Chain A   (BP45_BPMU | Q9T1V4)
molecular function
    GO:0046872    metal ion binding    Interacting selectively and non-covalently with any metal ion.
biological process
    GO:0046718    viral entry into host cell    The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the viral nucleic acid is released into the host cell cytoplasm.
    GO:0019076    viral release from host cell    The dissemination of mature viral particles from the host cell, e.g. by cell lysis or the budding of virus particles from the cell membrane.
cellular component
    GO:0030430    host cell cytoplasm    The cytoplasm of a host cell.
    GO:0019012    virion    The complete fully infectious extracellular virus particle.

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  3vtn
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 Related Entries

(-) Entries Sharing at Least One Protein Chain (UniProt ID)

UniProtKB/Swiss-Prot
        BP45_BPMU | Q9T1V4: 3vto

(-) Related Entries Specified in the PDB File

3vto