9GBN

Human Angiotensin-1 converting enzyme C-domain in complex with a diprolyl inhibitor- SG15

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 (D)	2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-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		1463.3	1	In PDB GlyTouCan (G80858MF)
3	C (A)	2-acetamido-2-deoxy-beta-D-glucopyranose	non-polymer		221.2	1	Chemie (NAG)
4	D (A)	1,2-ETHANEDIOL	non-polymer		62.1	1	Chemie (EDO)
5	E (A)	ZINC ION	non-polymer		65.4	1	Chemie (ZN)
6	F, G (A)	CHLORIDE ION	non-polymer		35.5	2	Chemie (CL)
7	H (A)	(2S)-1-[(2S)-2-[[(1S)-1-[(2S)-1-[(2S)-2-azanyl-3-phenyl-propanoyl]pyrrolidin-2-yl]-2-oxidanyl-2-oxidanylidene-ethyl]amino]propanoyl]pyrrolidine-2-carboxylic acid	non-polymer		460.5	1	Chemie (A1IJZ)
8	I (A)	water	water		18.0	334	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	1463.3
Non-Polymers*	Number of molecules	6
	Total formula weight	880.1
All*	Total formula weight	71205.3

*Water molecules are not included.