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1UZC

THE STRUCTURE OF AN FF DOMAIN FROM HUMAN HYPA/FBP11

Replaces:  1H40
Summary for 1UZC
Entry DOI10.2210/pdb1uzc/pdb
DescriptorHYPOTHETICAL PROTEIN FLJ21157 (1 entity in total)
Functional Keywordsnuclear protein, transcription, phosphopeptide recognition, rna polymerase ii carboxyl-terminal domain
Biological sourceHOMO SAPIENS (HUMAN)
Total number of polymer chains1
Total formula weight8251.47
Authors
Allen, M.D.,Jemth, P.,Friedler, A.,Schon, O.,Bycroft, M. (deposition date: 2004-03-09, release date: 2004-04-05, Last modification date: 2024-05-15)
Primary citationAllen, M.D.,Friedler, A.,Schon, O.,Bycroft, M.
The Structure of an Ff Domain from Human Hypa/Fbp11.
J.Mol.Biol., 323:411-416, 2002
Cited by
PubMed Abstract: The FF domain is a 60 amino acid residue phosphopeptide-binding module found in a variety of eukaryotic proteins including the transcription elongation factor CA150, the splicing factor Prp40 and p190RHOGAP. We have determined the structure of an FF domain from HYPA/FBP11. The domain is composed of three alpha helices arranged in an orthogonal bundle with a 3(10) helix in the loop between the second and third alpha helices. The structure differs from those of other phosphopeptide-binding domains and represents a novel phosphopeptide-binding fold.
PubMed: 12381297
DOI: 10.1016/S0022-2836(02)00968-3
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

237735

数据于2025-06-18公开中

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