6EN5: Angiotensin-converting enzyme

Crystal structure A of the Angiotensin-1 converting enzyme N-domain in complex with a diprolyl inhibitor. Determined by X-ray diffraction at 1.75 Å resolution. Released 20 Dec 2017.

Method
X-ray diffraction
Resolution
1.75 Å
Organism
Homo sapiens
Chains
4
Atoms
23,529
Mol. weight
304.58 kDa
Ligands
BJ2, ZN, XPE, PE3
Released
20 Dec 2017

Explore 6EN5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6EN5 contains 153 α-helices and 28 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 38 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix3-53
α-helix14-4330
α-helix48-7629
α-helix80-823
α-helix86-9510
α-helix99-1024
α-helix105-12420
β-strand126-12721
β-strand137-13821
α-helix139-1435
α-helix144-1496
α-helix153-16311
α-helix164-1685
α-helix169-18719
α-helix194-2007
α-helix207-23731
α-helix2471
β-strand248-24922
α-helix262-2643
α-helix265-2684
α-helix280-2856
α-helix290-30314
α-helix307-3104
α-helix311-3166
β-strand31813
β-strand333-33643
β-strand343-34643
α-helix353-37220
α-helix377-3793
α-helix385-39915
α-helix402-4076
α-helix418-43215
α-helix435-45117
α-helix456-4583
α-helix459-4668
α-helix467-4715
β-strand473-47422
α-helix485-4884
α-helix499-51820
α-helix525-5273
α-helix534-54512
α-helix552-5609
α-helix568-58720
α-helix590-5912
α-helix601-6044
Chain B: 40 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix3-53
α-helix14-4330
α-helix48-7629
α-helix80-823
α-helix86-9510
α-helix99-1024
α-helix105-12420
β-strand12714
α-helix1361
β-strand13714
α-helix1381
α-helix139-1435
α-helix144-1496
α-helix153-16311
α-helix164-1685
α-helix169-18719
α-helix194-2007
α-helix207-23731
α-helix2471
β-strand248-24925
α-helix262-2643
α-helix265-2684
α-helix280-2856
α-helix290-30314
α-helix307-3104
α-helix311-3166
β-strand31816
β-strand333-33646
β-strand343-34646
α-helix353-37119
α-helix377-3793
α-helix385-39915
α-helix402-4076
α-helix418-43215
α-helix435-45117
α-helix456-4583
α-helix459-4668
α-helix467-4715
β-strand473-47425
α-helix485-4884
α-helix499-51820
α-helix525-5273
α-helix534-54613
α-helix552-5609
α-helix568-58720
α-helix590-5912
α-helix601-6044
Chain C: 38 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix3-53
α-helix14-4330
α-helix48-7629
α-helix80-823
α-helix86-9510
α-helix99-1024
α-helix105-12420
β-strand127-12827
β-strand136-13727
α-helix139-1435
α-helix144-1496
α-helix153-16311
α-helix164-1685
α-helix169-18719
α-helix194-2007
α-helix207-23731
α-helix2471
β-strand248-24928
α-helix262-2643
α-helix265-2684
α-helix280-2856
α-helix290-30314
α-helix307-3104
α-helix311-3166
β-strand31819
β-strand333-33649
β-strand343-34649
α-helix353-37119
α-helix377-3793
α-helix385-39915
α-helix402-4076
α-helix418-43215
α-helix435-45117
α-helix456-4583
α-helix459-4668
α-helix467-4715
β-strand473-47428
α-helix485-4884
α-helix499-51820
α-helix525-5273
α-helix534-54613
α-helix552-5609
α-helix568-58720
α-helix590-5912
α-helix601-6044
Chain D: 37 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix3-53
α-helix14-4330
α-helix48-7629
α-helix80-823
α-helix86-9510
α-helix99-1024
α-helix105-12420
β-strand126-128310
β-strand136-138310
α-helix139-1435
α-helix144-1496
α-helix153-18735
α-helix194-2007
α-helix207-23731
α-helix2471
β-strand248-249211
α-helix262-2643
α-helix265-2684
α-helix280-2856
α-helix290-30314
α-helix307-3104
α-helix311-3166
β-strand318112
β-strand333-336412
β-strand343-346412
α-helix353-37119
α-helix377-3793
α-helix385-39915
α-helix402-4076
α-helix418-43215
α-helix435-45117
α-helix456-4583
α-helix459-4668
α-helix467-4715
β-strand473-474211
α-helix485-4884
α-helix499-51820
α-helix525-5273
α-helix534-54613
α-helix552-5609
α-helix568-58720
α-helix590-5912
α-helix601-6044
α-helix609-6135

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Angiotensin-converting enzymeA, B, C, Dprotein629Homo sapiensP12821 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>6EN5_1 Angiotensin-converting enzyme (chains A, B, C, D)
LDPGLQPGQFSADEAGAQLFAQSYQSSAEQVLFQSVAASWAHDTNITAENARRQEEAALL
SQEFAEAWGQKAKELYEPIWQQFTDPQLRRIIGAVRTLGSANLPLAKRQQYNALLSQMSR
IYSTAKVCLPQKTATCWSLDPDLTNILASSRSYAMLLFAWEGWHNAAGIPLKPLYEDFTA
LSNEAYKQDGFTDTGAYWRSWYNSPTFEDDLEHLYQQLEPLYLNLHAFVRRALHRRYGDR
YINLRGPIPAHLLGDMWAQSWENIYDMVVPFPDKPNLDVTSTMLQQGWQATHMFRVAEEF
FTSLELSPMPPEFWEGSMLEKPADGREVVCHASAWDFYNRKDFRIKQCTRVTMDQLSTVH
HEMGHIQYYLQYKDLPVSLRRGANPGFHEAIGDVLALSVSTPEHLHKIGLLDRVTNDTES
DINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPPSRYNFDWWYLRTKYQGICPPVTRN
ETHFDAGAKFHVPNVTPYIRYFVSFVLQFQFHEALCKEAGYEGPLHQCDIYRSTKAGAKL
RKVLRAGSSRPWQEVLKDMVGLDALDAQPLLKYFQLVTQWLQEQNQQNGEVLGWPEYQWH
PPLPDNYPEGIDLVTDEAEASKFVEEYDL

Ligands and cofactors

IDNameFormulaCopies
BJ2(2~{S})-1-[(2~{S})-2-[[(1~{S})-1-[(2~{S})-1-[(2~{S})-2-azanyl-4-oxidanyl-4-oxid…C18 H28 N4 O84
ZNZinc ionZn4
XPE3,6,9,12,15,18,21,24,27-nonaoxanonacosane-1,29-diolC20 H42 O111
PE33,6,9,12,15,18,21,24,27,30,33,36,39-tridecaoxahentetracontane-1,41-diolC28 H58 O151
MGMagnesium ionMg4

Water and common crystallization additives (CL, PG4, PGE, ACT, EDO, PEG) are not listed.

Primary citation

The Design and Development of a Potent and Selective Novel Diprolyl Derivative That Binds to the N-Domain of Angiotensin-I Converting Enzyme. Fienberg, S., Cozier, G.E., Acharya, K.R. et al. J Med Chem (2018) 61:344-359. DOI 10.1021/acs.jmedchem.7b01478 · PubMed

Other PDB entries of the same protein (UniProt P12821 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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