9H1C

Crystal structure of Angiotensin-1 converting enzyme C-domain in complex with dual ACE/NEP inhibitor AD014

This is a non-PDB format compatible entry.

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)-[alpha-D-mannopyranose-(1-6)]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		1057.0	1	In PDB GlyTouCan (G82348BZ)
3	C (A)	(2~{S},5~{R})-5-(3-hydroxyphenyl)-1-[2-[[(2~{S})-3-(4-hydroxyphenyl)-2-sulfanyl-propanoyl]amino]ethanoyl]pyrrolidine-2-carboxylic acid	non-polymer		444.5	1	Chemie (A1IRQ)
4	D, E, F (A)	BORIC ACID	non-polymer		61.8	3	Chemie (BO3)
5	G (A)	TRIETHYLENE GLYCOL	non-polymer		150.2	1	Chemie (PGE)
6	H (A)	IMIDAZOLE	non-polymer		69.1	1	Chemie (IMD)
7	I, J (A)	1,2-ETHANEDIOL	non-polymer		62.1	2	Chemie (EDO)
8	K (A)	2-acetamido-2-deoxy-beta-D-glucopyranose	non-polymer		221.2	1	Chemie (NAG)
9	L (A)	ZINC ION	non-polymer		65.4	1	Chemie (ZN)
10	M, N (A)	CHLORIDE ION	non-polymer		35.5	2	Chemie (CL)
11	O (A)	water	water		18.0	501	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	1057.0
Non-Polymers*	Number of molecules	12
	Total formula weight	1330.9
All*	Total formula weight	71249.8

*Water molecules are not included.