7Q28

Crystal structure of Angiotensin-1 converting enzyme C-domain in complex with dual ACE/NEP inhibitor AD012

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A (A)	Angiotensin-converting enzyme	polymer	597	68861.9	1	UniProt (P12821) Pfam (PF01401)	Homo sapiens (Human)	ACE,Dipeptidyl carboxypeptidase I,Kininase II
2	B (B)	alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose	branched		894.8	1	In PDB GlyTouCan (G42466VF)
3	C (A)	2-acetamido-2-deoxy-beta-D-glucopyranose	non-polymer		221.2	1	Chemie (NAG)
4	D, H, J (A)	BORIC ACID	non-polymer		61.8	3	Chemie (BO3)
5	E (A)	(2~{S})-2-[[(2~{S})-1-[[(2~{S})-3-(4-hydroxyphenyl)-1-oxidanyl-1-oxidanylidene-propan-2-yl]amino]-1-oxidanylidene-hexan-2-yl]amino]-4-phenyl-butanoic acid	non-polymer		456.5	1	Chemie (8J9)
6	F (A)	DI(HYDROXYETHYL)ETHER	non-polymer		106.1	1	Chemie (PEG)
7	G, I (A)	1,2-ETHANEDIOL	non-polymer		62.1	2	Chemie (EDO)
8	K (A)	ZINC ION	non-polymer		65.4	1	Chemie (ZN)
9	L, M (A)	CHLORIDE ION	non-polymer		35.5	2	Chemie (CL)
10	N (A)	water	water		18.0	434	Chemie (HOH)

Sequence modifications

A: 37 - 633 (UniProt: P12821)

PDB	External Database	Details
Gly 64	Glu 669	engineered mutation
Gln 90	Asn 695	engineered mutation
Gln 155	Asn 760	engineered mutation
Gln 337	Asn 942	engineered mutation
Gln 586	Asn 1191	engineered mutation

Contents of the asymmetric unit

Polymers	Number of chains	1
	Total formula weight	68861.9
Branched	Number of molecules	1
	Total formula weight	894.8
Non-Polymers*	Number of molecules	11
	Total formula weight	1229.8
All*	Total formula weight	70986.5

*Water molecules are not included.