6LT4
AAA+ ATPase, ClpL from Streptococcus pneumoniae: ATPrS-bound
Summary for 6LT4
Entry DOI | 10.2210/pdb6lt4/pdb |
EMDB information | 0967 |
Descriptor | ATP-dependent Clp protease, ATP-binding subunit, MAGNESIUM ION, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER (3 entities in total) |
Functional Keywords | aaa+ atpase, chaperone, clpl, streptococcus pneumoniae |
Biological source | Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) |
Total number of polymer chains | 14 |
Total formula weight | 1101718.77 |
Authors | Kim, G.,Lee, S.G.,Han, S.,Jung, J.,Jeong, H.S.,Hyun, J.K.,Rhee, D.K.,Kim, H.M.,Lee, S. (deposition date: 2020-01-21, release date: 2021-01-27, Last modification date: 2024-03-27) |
Primary citation | Kim, G.,Lee, S.G.,Han, S.,Jung, J.,Jeong, H.S.,Hyun, J.K.,Rhee, D.K.,Kim, H.M.,Lee, S. ClpL is a functionally active tetradecameric AAA+ chaperone, distinct from hexameric/dodecameric ones. Faseb J., 34:14353-14370, 2020 Cited by PubMed: 32910525DOI: 10.1096/fj.202000843R PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.5 Å) |
Structure validation
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