3HLN

Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A, B, C, D, E...	ATP-dependent Clp protease proteolytic subunit	polymer	193	21618.9	28	UniProt (P0A6G7) Pfam (PF00574) In PDB	Escherichia coli	Endopeptidase Clp, Caseinolytic protease, Protease Ti, Heat shock protein F21.5
2	E, I, J, M, T...	CALCIUM ION	non-polymer		40.1	13	Chemie (CA)

Sequence modifications

A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, 1, 2: 1 - 193 (UniProt: P0A6G7)

PDB	External Database	Details
Cys 139	Ala 153	engineered mutation

Contents of the asymmetric unit

Polymers	Number of chains	28
	Total formula weight	605330.0
Non-Polymers*	Number of molecules	13
	Total formula weight	521.0
All*	Total formula weight	605851.0

*Water molecules are not included.