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2VFN

Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V125A

Summary for 2VFN
Entry DOI10.2210/pdb2vfn/pdb
Related1CLW 1LKT 1QA1 1QA2 1QA3 1QQ1 1QRB 1QRC 1TSP 1TYV 2VFM 2VFO 2VFP 2VFQ
DescriptorBIFUNCTIONAL TAIL PROTEIN, GLYCEROL, SULFATE ION, ... (5 entities in total)
Functional Keywordsp22 tailspike protein, salmonella bacteriophage p22, protein folding, protein stability, right-handed parallel beta-helix, hydrolase, late protein, endoglycosidase
Biological sourceENTEROBACTERIA PHAGE P22 (BACTERIOPHAGE P22)
Cellular locationVirion (Potential): P12528
Total number of polymer chains1
Total formula weight61262.32
Authors
Becker, M.,Mueller, J.J.,Heinemann, U.,Seckler, R. (deposition date: 2007-11-05, release date: 2008-12-16, Last modification date: 2023-12-13)
Primary citationBecker, M.,Mueller, J.J.,Weikl, T.,Heinemann, U.,Seckler, R.
Side-Chain Stacking and Beta-Helix Stability in P22 Tailspike Protein
To be Published,
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

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