Show PDB file:   
         Plain Text   HTML   (compressed file size)
QuickSearch:   
by PDB,NDB,UniProt,PROSITE Code or Search Term(s)  
(-)Asymmetric Unit
(-)Biological Unit 1
collapse expand < >
Image Asymmetric Unit
Asymmetric Unit  (Jmol Viewer)
Image Biological Unit 1
Biological Unit 1  (Jmol Viewer)

(-) Description

Title :  THE CRYSTAL STRUCTURE OF THE PRRSV NONSTRUCTURAL PROTEIN NSP1
 
Authors :  F. Xue, Y. N. Sun, L. M. Yan, C. Zhao, Z. Y. Lou, Z. H. Rao
Date :  30 Apr 10  (Deposition) - 19 May 10  (Release) - 21 Jul 10  (Revision)
Method :  X-RAY DIFFRACTION
Resolution :  2.80
Chains :  Asym. Unit :  A
Biol. Unit 1:  A  (2x)
Keywords :  Prrsv, Nsp1, Nuclease, Papain-Like Cysteine Protease, Hydrolase (Keyword Search: [Gene Ontology, PubMed, Web (Google))
 
Reference :  F. Xue, Y. N. Sun, L. M. Yan, C. Zhao, J. Chen, M. Bartlam, X. M. Li, Z. Y. Lou, Z. H. Rao
The Crystal Structure Of Porcine Reproductive And Respiratory Syndrome Virus Nonstructural Protein Nsp1Beta Reveals A Novel Metal-Dependent Nuclease
J. Virol. V. 84 6461 2010
PubMed-ID: 20410261  |  Reference-DOI: 10.1128/JVI.00301-10

(-) Compounds

Molecule 1 - PAPAIN-LIKE CYSTEINE PROTEASE
    ChainsA
    EngineeredYES
    Expression SystemESCHERICHIA COLI
    Expression System PlasmidPGEX-6P-1
    Expression System StrainBL21 (DE3)
    Expression System Taxid469008
    Expression System Vector TypePLASMID
    FragmentUNP RESIDUES 181-383
    Organism CommonPRRSV
    Organism ScientificPORCINE REPRODUCTIVE AND RESPIRATORY SYNDROME VIRUS
    Organism Taxid28344
    SynonymNSP1B

 Structural Features

(-) Chains, Units

  1
Asymmetric Unit A
Biological Unit 1 (2x)A

Summary Information (see also Sequences/Alignments below)

(-) Ligands, Modified Residues, Ions  (0, 0)

(no "Ligand,Modified Residues,Ions" information available for 3MTV)

(-) Sites  (0, 0)

(no "Site" information available for 3MTV)

(-) SS Bonds  (0, 0)

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

(-) Cis Peptide Bonds  (0, 0)

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

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 3MTV)

(-) PROSITE Motifs  (0, 0)

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

(-) Exons   (0, 0)

(no "Exon" information available for 3MTV)

(-) Sequences/Alignments

Asymmetric Unit
   Reformat: Number of residues per line =  ('0' or empty: single-line sequence representation)
  Number of residues per labelling interval =   
  UniProt sequence: complete  aligned part    
   Show mapping: SCOP domains CATH domains Pfam domains Secondary structure (by author)
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:203
 aligned with B2ZAB4_PRRSV | B2ZAB4 from UniProtKB/TrEMBL  Length:2473

    Alignment length:203
                                   190       200       210       220       230       240       250       260       270       280       290       300       310       320       330       340       350       360       370       380   
         B2ZAB4_PRRSV   181 ADVYDIGRGAVMYVAGGKVSWAPRGGNEVKFEPVPKELKLVANRLHTSFPPHHVVDMSKFTFITPGSGVSMRVEYQYGCLPADTVPEGNCWWRLLDSLPPEVQYKEIRHANQFGYQTKHGVPGKYLQRRLQVNGLRAVTDTHGPIVIQYFSVKESWIRHLKLVEEPSLPGFEDLLRIRVEPNTSPLAGKDEKIFRFGSHKWYG 383
               SCOP domains ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains --------------------------------------------------------------------------Peptidase_C32-3mtvA01 A:75-202                                                                                                  - Pfam domains
         Sec.struct. author ..eeeee..eeeeee..eeeeee..............hhhhhhhhhhhh....eee.hhh.......ee.......ee..hhhhh.....hhhhhh..hhhhhhhhhhhhhhh.........hhhhhhhhhh..eeeee.....eeeeee.......eeeee........eeeeeeeeeee..........ee.......... Sec.struct. author
                 SAPs(SNPs) ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 3mtv A   1 ADVYDIGRGAVMYVAGGKVSWAPRGGNEVKFEPVPKELKLVANRLHTSFPPHHVVDMSKFTFITPGSGVSMRVEYQYGCLPADTVPEGNCWWRLLDSLPPEVQYKEIRHANQFGYQTKHGVPGKYLQRRLQVNGLRAVTDTHGPIVIQYFSVKESWIRHLKLVEEPSLPGFEDLLRIRVEPNTSPLAGKDEKIFRFGSHKWYG 203
                                    10        20        30        40        50        60        70        80        90       100       110       120       130       140       150       160       170       180       190       200   

   Legend:   → Mismatch (orange background)
  - → Gap (green background, '-', border residues have a numbering label)
    → Modified Residue (blue background, lower-case, 'x' indicates undefined single-letter code, labelled with number + name)
  x → Chemical Group (purple background, 'x', labelled with number + name, e.g. ACE or NH2)
  extra numbering lines below/above indicate numbering irregularities and modified residue names etc., number ends below/above '|'

 Classification and Annotation

(-) SCOP Domains  (0, 0)

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

(-) CATH Domains  (0, 0)

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

(-) Pfam Domains  (1, 1)

Asymmetric Unit

(-) Gene Ontology  (9, 9)

Asymmetric Unit(hide GO term definitions)
Chain A   (B2ZAB4_PRRSV | B2ZAB4)
molecular function
    GO:0004197    cysteine-type endopeptidase activity    Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile.
    GO:0008234    cysteine-type peptidase activity    Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile.
    GO:0008233    peptidase activity    Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
    GO:0004252    serine-type endopeptidase activity    Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
biological process
    GO:0006508    proteolysis    The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
    GO:0016032    viral process    A multi-organism process in which a virus is a participant. The other participant is the host. Includes infection of a host cell, replication of the viral genome, and assembly of progeny virus particles. In some cases the viral genetic material may integrate into the host genome and only subsequently, under particular circumstances, 'complete' its life cycle.
    GO:0019082    viral protein processing    Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a viral protein.
cellular component
    GO:0016021    integral component of membrane    The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
    GO:0016020    membrane    A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

 Visualization

(-) Interactive Views

Asymmetric Unit
  Complete Structure
    Jena3D(integrated viewing of ligand, site, SAP, PROSITE, SCOP information)
    WebMol | AstexViewer[tm]@PDBe
(Java Applets, require no local installation except for Java; loading may be slow)
    STRAP
(Java WebStart application, automatic local installation, requires Java; full application with system access!)
    RasMol
(require local installation)
    Molscript (VRML)
(requires installation of a VRML viewer; select preferred view via VRML and generate a mono or stereo PDF format file)
 
  Ligands, Modified Residues, Ions
(no "Ligands, Modified Residues, Ions" information available for 3mtv)
 
  Sites
(no "Sites" information available for 3mtv)
 
  Cis Peptide Bonds
(no "Cis Peptide Bonds" information available for 3mtv)
 
Biological Unit
  Complete Structure
    Biological Unit 1  [ Jena3D ]

(-) Still Images

Jmol
  protein: cartoon or spacefill or dots and stick; nucleic acid: cartoon and stick; ligands: spacefill; active site: stick
Molscript
  protein, nucleic acid: cartoon; ligands: spacefill; active site: ball and stick

 Databases and Analysis Tools

(-) Databases

Access by PDB/NDB ID
  3mtv
    Family and Domain InformationProDom | SYSTERS
    General Structural InformationGlycoscienceDB | MMDB | NDB | OCA | PDB | PDBe | PDBj | PDBsum | PDBWiki | PQS | PROTEOPEDIA
    Orientation in MembranesOPM
    Protein SurfaceSURFACE
    Secondary StructureDSSP (structure derived) | HSSP (homology derived)
    Structural GenomicsGeneCensus
    Structural NeighboursCE | VAST
    Structure ClassificationCATH | Dali | SCOP
    Validation and Original DataBMRB Data View | BMRB Restraints Grid | EDS | PROCHECK | RECOORD | WHAT_CHECK
 
Access by UniProt ID/Accession number
  B2ZAB4_PRRSV | B2ZAB4
    Comparative Protein Structure ModelsModBase
    Genomic InformationEnsembl
    Protein-protein InteractionDIP
    Sequence, Family and Domain InformationInterPro | Pfam | SMART | UniProtKB/TrEMBL
 
Access by Enzyme Classificator   (EC Number)
  (no 'Enzyme Classificator' available)
    General Enzyme InformationBRENDA | EC-PDB | Enzyme | IntEnz
    PathwayKEGG | MetaCyc
 
Access by Disease Identifier   (MIM ID)
  (no 'MIM ID' available)
    Disease InformationOMIM
 
Access by GenAge ID
  (no 'GenAge ID' available)
    Age Related InformationGenAge

(-) Analysis Tools

Access by PDB/NDB ID
    Domain InformationXDom
    Interatomic Contacts of Structural UnitsCSU
    Ligand-protein ContactsLPC
    Protein CavitiescastP
    Sequence and Secondary StructurePDBCartoon
    Structure AlignmentSTRAP(Java WebStart application, automatic local installation, requires Java; full application with system access!)
    Structure and Sequence BrowserSTING
 
Access by UniProt ID/Accession number
  B2ZAB4_PRRSV | B2ZAB4
    Protein Disorder PredictionDisEMBL | FoldIndex | GLOBPLOT (for more information see DisProt)

 Related Entries

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

(no "Entries Sharing at Least One Protein Chain" available for 3MTV)

(-) Related Entries Specified in the PDB File

(no "Related Entries Specified in the PDB File" available for 3MTV)