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PDBe Entry: 1g31 view

GP31 CO-CHAPERONIN FROM BACTERIOPHAGE T4
Summary
Header CHAPERONEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.3 Å, R-factor: 22.5%, Free R-factor: 25.4%, Spacegroup: P 42 21 2
Released 26/08/1998, deposition: 27/03/1998, last revision: 24/02/2009
Authors Hunt, J.F.search; Van Der Vies, S.M.search; Henry, L.search; Deisenhofer, J.search
Primary citation Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen cage.
CELL(CAMBRIDGE,MASS.)search vol:90, pag:361-371 (1997) [PubMed ID 9244309 ]search
Keywords CHAPERONEsearch, CO-CHAPERONINsearch, GROESsearch, IN VIVO PROTEIN FOLDINGsearch, BACTERIOPHAGE T4search
Organism Enterobacteria phage T4 10665search(A B C D E F G)
UniProt Capsid assembly protein Gp31 P17313search (A B C D E F G)
Solvent A, B, C, D, E, F, G
Polymers
Id Name Type UniProt Residues Observed
A, B, C, D, E, F, G GP31 Protein P17313 (VG31_BPT4)search
111 96%
Heterogens
Id Name Ligands
A, B, C, D, E, F, G PHOSPHATE ION PO4 search
A, B, C, D, E, F, G POTASSIUM ION K search
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