1ocy

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File:1ocy.png


PDB ID 1ocy

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1ocy, resolution 1.50Å ()
Ligands: , ,
Related: 1h6w
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF THE RECEPTOR-BINDING DOMAIN OF THE BACTERIOPHAGE T4 SHORT TAIL FIBRESTRUCTURE OF THE RECEPTOR-BINDING DOMAIN OF THE BACTERIOPHAGE T4 SHORT TAIL FIBRE

Template:ABSTRACT PUBMED 12888344

About this StructureAbout this Structure

1ocy is a 1 chain structure with sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1][xtra 2][xtra 3][xtra 4][xtra 5]

  1. Thomassen E, Gielen G, Schutz M, Schoehn G, Abrahams JP, Miller S, van Raaij MJ. The structure of the receptor-binding domain of the bacteriophage T4 short tail fibre reveals a knitted trimeric metal-binding fold. J Mol Biol. 2003 Aug 8;331(2):361-73. PMID:12888344
  2. van Raaij MJ, Schoehn G, Burda MR, Miller S. Crystal structure of a heat and protease-stable part of the bacteriophage T4 short tail fibre. J Mol Biol. 2001 Dec 14;314(5):1137-46. PMID:11743729 doi:10.1006/jmbi.2000.5204
  3. van Raaij MJ, Schoehn G, Jaquinod M, Ashman K, Burda MR, Miller S. Identification and crystallisation of a heat- and protease-stable fragment of the bacteriophage T4 short tail fibre. Biol Chem. 2001 Jul;382(7):1049-55. PMID:11530935 doi:10.1515/BC.2001.131
  4. Burda MR, Hindennach I, Miller S. Stability of bacteriophage T4 short tail fiber. Biol Chem. 2000 Mar;381(3):255-8. PMID:10782996 doi:10.1515/BC.2000.032
  5. Burda MR, Miller S. Folding of coliphage T4 short tail fiber in vitro. Analysing the role of a bacteriophage-encoded chaperone. Eur J Biochem. 1999 Oct;265(2):771-8. PMID:10504409

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