4AON

Conformational dynamics of aspartate alpha-decarboxylase active site revealed by protein-ligand complexes: 1-methyl-L-aspartate complex

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A, D	ASPARTATE-ALPHA-DECARBOXYLASE BETA CHAIN	polymer	41	4770.6	2	UniProt (P0A790) In PDB	ESCHERICHIA COLI
2	B, E	ASPARTATE-ALPHA-DECARBOXYLASE ALPHA CHAIN	polymer	102	11010.3	2	UniProt (P0A790) Pfam (PF02261) In PDB	ESCHERICHIA COLI
3	B, E	GLUTAMIC ACID	non-polymer		147.1	2	Chemie (GLU)
4		water	water		18.0	203	Chemie (HOH)

Sequence modifications

A, D: 1 - 24 (UniProt: P0A790)

PDB	External Database	Details
Met -16	-	expression tag
Arg -15	-	expression tag
Gly -14	-	expression tag
Ser -13	-	expression tag
His -12	-	expression tag
His -11	-	expression tag
His -10	-	expression tag
His -9	-	expression tag
His -8	-	expression tag
His -7	-	expression tag
Gly -6	-	expression tag
Leu -5	-	expression tag
Val -4	-	expression tag
Pro -3	-	expression tag
Arg -2	-	expression tag
Gly -1	-	expression tag
Ser 0	-	expression tag

B, E: 25 - 126 (UniProt: P0A790)

PDB	External Database	Details
Pyr 25	Ser 25	microheterogeneity

Contents of the asymmetric unit

Polymers	Number of chains	4
	Total formula weight	31561.8
Non-Polymers*	Number of molecules	2
	Total formula weight	294.3
All*	Total formula weight	31856.0

*Water molecules are not included.