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: 32910525 DOI: 10.1096/fj.202000843R PDB entries with the same primary citation
Experimental method	ELECTRON MICROSCOPY (4.5 Å)

Structure validation