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7OC9

Structure of Bdellovibrio bacteriovorus Bd0675

Summary for 7OC9
Entry DOI10.2210/pdb7oc9/pdb
DescriptorBd0675, (4S)-2-METHYL-2,4-PENTANEDIOL, GLYCEROL, ... (5 entities in total)
Functional Keywordsbdellovibrio secretion cryptic, unknown function
Biological sourceBdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100)
Total number of polymer chains1
Total formula weight15198.15
Authors
Lovering, A.L.,Valdivia-Delgado, M. (deposition date: 2021-04-26, release date: 2021-05-05, Last modification date: 2024-10-09)
Primary citationAlexander, L.T.,Lepore, R.,Kryshtafovych, A.,Adamopoulos, A.,Alahuhta, M.,Arvin, A.M.,Bomble, Y.J.,Bottcher, B.,Breyton, C.,Chiarini, V.,Chinnam, N.B.,Chiu, W.,Fidelis, K.,Grinter, R.,Gupta, G.D.,Hartmann, M.D.,Hayes, C.S.,Heidebrecht, T.,Ilari, A.,Joachimiak, A.,Kim, Y.,Linares, R.,Lovering, A.L.,Lunin, V.V.,Lupas, A.N.,Makbul, C.,Michalska, K.,Moult, J.,Mukherjee, P.K.,Nutt, W.S.,Oliver, S.L.,Perrakis, A.,Stols, L.,Tainer, J.A.,Topf, M.,Tsutakawa, S.E.,Valdivia-Delgado, M.,Schwede, T.
Target highlights in CASP14: Analysis of models by structure providers.
Proteins, 89:1647-1672, 2021
Cited by
PubMed Abstract: The biological and functional significance of selected Critical Assessment of Techniques for Protein Structure Prediction 14 (CASP14) targets are described by the authors of the structures. The authors highlight the most relevant features of the target proteins and discuss how well these features were reproduced in the respective submitted predictions. The overall ability to predict three-dimensional structures of proteins has improved remarkably in CASP14, and many difficult targets were modeled with impressive accuracy. For the first time in the history of CASP, the experimentalists not only highlighted that computational models can accurately reproduce the most critical structural features observed in their targets, but also envisaged that models could serve as a guidance for further studies of biologically-relevant properties of proteins.
PubMed: 34561912
DOI: 10.1002/prot.26247
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

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