Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

9SFA

Cyclic nucleotide binding transcription factor Bd2879 - apo form

Summary for 9SFA
Entry DOI10.2210/pdb9sfa/pdb
DescriptorPutative regulatory protein (1 entity in total)
Functional Keywordscyclic nucleotide binding, transcription factor, dimer, complex, helix-turn-helix, signaling protein
Biological sourceBdellovibrio bacteriovorus HD100
Total number of polymer chains2
Total formula weight87178.40
Authors
Jenkins, M.R.,Box, H.,Caulton, S.G.,Lovering, A.L. (deposition date: 2025-08-19, release date: 2025-10-22)
Primary citationAlexander, L.T.,Follonier, O.M.,Kryshtafovych, A.,Abesamis, K.,Bibi-Triki, S.,Box, H.G.,Breyton, C.,Bringel, F.,Carrique, L.,d'Acapito, A.,Dong, G.,DuBois, R.,Fass, D.,Fiesco, J.M.,Fox, D.R.,Grimes, J.M.,Grinter, R.,Jenkins, M.,Kamyshinsky, R.,Keown, J.R.,Lackner, G.,Lammers, M.,Liu, S.,Lovering, A.L.,Malinauskas, T.,Masquida, B.,Palm, G.J.,Siebold, C.,Su, T.,Zhang, P.,Zhou, Z.H.,Fidelis, K.,Topf, M.,Moult, J.,Schwede, T.
Protein Target Highlights in CASP16: Insights From the Structure Providers.
Proteins, 2025
Cited by
PubMed Abstract: This article presents an in-depth analysis of selected CASP16 targets, with a focus on their biological and functional significance. The authors highlight the most relevant features of the target proteins and discuss how well these were reproduced in the submitted predictions. While the overall performance of structure prediction methods remains impressive, challenges persist, particularly in modeling rare structural motifs, flexible regions, small molecule interactions, posttranslational modifications, and biologically important interfaces. Addressing these limitations can strengthen the role of structure prediction in complementing experimental efforts and advancing both basic research and biomedical applications.
PubMed: 41065010
DOI: 10.1002/prot.70025
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.88 Å)
Structure validation

245663

数据于2025-12-03公开中

PDB statisticsPDBj update infoContact PDBjnumon