2ASV

X-Ray studies on protein complexes: Enzymatic catalysis in Crystals of E. coli Maltodextrin Phosphorylase (MalP)

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A, B (A, B)	Maltodextrin phosphorylase	polymer	796	90547.1	2	UniProt (P00490) Pfam (PF00343)	Escherichia coli
2	C, D (C, D)	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose	branched		828.7	2	In PDB GlyTouCan (G43441FW)
3	E, H (A, B)	1,5-anhydro-D-glucitol	non-polymer		164.2	2	Chemie (ASO)
4	F, I (A, B)	PHOSPHATE ION	non-polymer		95.0	2	Chemie (PO4)
5	G, J (A, B)	PYRIDOXAL-5'-PHOSPHATE	non-polymer		247.1	2	Chemie (PLP)
6	K, L (A, B)	water	water		18.0	1184	Chemie (HOH)

Sequence modifications

A, B: 1 - 796 (UniProt: P00490)

PDB	External Database	Details
Ala 261	His 261	engineered mutation
Phe 262	Thr 262	engineered mutation
Glu 263	Ala 263	engineered mutation

Contents of the asymmetric unit

Polymers	Number of chains	2
	Total formula weight	181094.1
Branched	Number of molecules	2
	Total formula weight	1657.4
Non-Polymers*	Number of molecules	6
	Total formula weight	1012.5
All*	Total formula weight	183764.1

*Water molecules are not included.