5W1C

Crystal structure of MBP fused activation-induced cytidine deaminase (AID) in complex with cytidine

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	B, A	MBP fused activation-induced cytidine deaminase	polymer	549	62081.3	2	UniProt (P0AEY0) UniProt (Q9GZX7) Pfam (PF01547) Pfam (PF08210) UniProt (by SIFTS) (P0AEX9) In PDB	Escherichia coli O157:H7	MBP,MMBP,Maltodextrin-binding protein,Activation-induced cytidine deaminase,AID,Cytidine aminohydrolase
2	D	DNA (5'-D(*GP*TP*TP*CP*AP*AP*GP*GP*CP*CP*AP*G)-3')	polymer	12	3687.4	1		Homo sapiens
3	G	DNA (5'-D(*CP*TP*GP*GP*CP*CP*TP*TP*GP*AP*AP*C)-3')	polymer	12	3638.4	1		Homo sapiens
4	B, A	ZINC ION	non-polymer		65.4	2	Chemie (ZN)
5	B, A	4-AMINO-1-BETA-D-RIBOFURANOSYL-2(1H)-PYRIMIDINONE	non-polymer		243.2	2	Chemie (CTN)
6	B, A	CALCIUM ION	non-polymer		40.1	2	Chemie (CA)
7		water	water		18.0	2	Chemie (HOH)

Sequence modifications

B, A: 2 - 367 (UniProt: P0AEY0)

PDB	External Database	Details
Met 1	-	initiating methionine
Asn 368	-	linker
Ala 369	-	linker
Ala 370	-	linker
Ala 371	-	linker
Glu 372	-	linker

B, A: 373 - 1181 (UniProt: Q9GZX7)

PDB	External Database	Details
Phe 373	Leu 5	engineered mutation
Asp 1007	Asn 7	engineered mutation
Pro 1008	Arg 8	engineered mutation
Ala 1009	Arg 9	engineered mutation
Thr 1010	Lys 10	engineered mutation
Thr 1012	Leu 12	engineered mutation
Glu 1042	Phe 42	engineered mutation
Ala 1058	Glu 58	engineered mutation
Ala 1130	His 130	engineered mutation
Glu 1131	Arg 131	engineered mutation
Tyr 1141	Phe 141	engineered mutation
Glu 1145	Phe 145	engineered mutation
Gln 1181	Leu 181	engineered mutation

Contents of the asymmetric unit

Polymers	Number of chains	4
	Total formula weight	131488.4
Non-Polymers*	Number of molecules	6
	Total formula weight	697.4
All*	Total formula weight	132185.8

*Water molecules are not included.