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7Z70

Crystal structure of Angiotensin-1 converting enzyme C-domain in complex with fosinoprilat

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1A
(A)
Angiotensin-converting enzymepolymer59768877.91UniProt (P12821)
Pfam (PF01401)
Homo sapiens (human)ACE,Dipeptidyl carboxypeptidase I,Kininase II
2B
(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-glucopyranosebranched894.81In PDB
GlyTouCan (G42466VF)
3C
(A)
fosinoprilatnon-polymer435.51Chemie (KS8)
4D
(A)
2-acetamido-2-deoxy-beta-D-glucopyranosenon-polymer221.21Chemie (NAG)
5E, G
(A)
BORIC ACIDnon-polymer61.82Chemie (BO3)
6F
(A)
ACETATE IONnon-polymer59.01Chemie (ACT)
7H
(A)
IMIDAZOLEnon-polymer69.11Chemie (IMD)
8I, J, K
(A)
1,2-ETHANEDIOLnon-polymer62.13Chemie (EDO)
9L
(A)
ZINC IONnon-polymer65.41Chemie (ZN)
10M, N
(A)
CHLORIDE IONnon-polymer35.52Chemie (CL)
11O
(A)
waterwater18.0592Chemie (HOH)
Sequence modifications
A: 37 - 633 (UniProt: P12821)
PDBExternal DatabaseDetails
Gly 64Glu 669engineered mutation
Gln 90Asn 695engineered mutation
Gln 155Asn 760engineered mutation
Gln 337Asn 942engineered mutation
Gln 586Asn 1191engineered mutation
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains1
Total formula weight68877.9
BranchedNumber of molecules1
Total formula weight894.8
Non-Polymers*Number of molecules12
Total formula weight1231.0
All*Total formula weight71003.7
*Water molecules are not included.

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PDB entries from 2024-10-30

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