8QFX: Human Angiotensin-1 converting enzyme N-domain

Human Angiotensin-1 converting enzyme N-domain in complex with the lactotripeptide IPP. Determined by X-ray diffraction at 1.6 Å resolution. Released 22 Nov 2023.

Method
X-ray diffraction
Resolution
1.6 Å
Organisms
Homo sapiens, Bos taurus
Chains
8
Atoms
23,659
Mol. weight
303.89 kDa
Ligands
BMA, MG, ZN, FUC
Released
22 Nov 2023

Explore 8QFX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8QFX contains 150 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: 39 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
α-helix1361
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-helix280-2867
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-helix436-45116
α-helix456-4583
α-helix459-4668
α-helix467-4715
β-strand473-47422
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 B: 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-strand127-12824
β-strand136-13724
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-helix385-40016
α-helix402-4076
α-helix418-43215
α-helix436-45116
α-helix456-4583
α-helix459-47113
β-strand473-47425
α-helix485-4884
α-helix499-51921
α-helix525-5273
α-helix534-54613
α-helix552-5609
α-helix568-58720
α-helix590-5912
α-helix603-6042
α-helix609-6135
Chain C: 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-strand12717
β-strand13717
α-helix139-1435
α-helix144-1496
α-helix153-18735
α-helix194-2007
α-helix207-23731
α-helix2471
β-strand248-24928
α-helix262-2643
α-helix265-2684
α-helix280-2867
α-helix290-30314
α-helix307-3104
α-helix311-3166
β-strand31819
β-strand333-33649
β-strand343-34649
α-helix353-37220
α-helix377-3793
α-helix385-39915
α-helix402-4076
α-helix412-4154
α-helix418-43215
α-helix436-45116
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: 36 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-strand127-128210
β-strand136-137210
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-helix280-2867
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-helix436-45116
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

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Angiotensin-converting enzyme, soluble formA, B, C, Dprotein628Homo sapiensP12821 (AlphaFold model)
Ile-pro-proE, F, G, Hprotein3Bos taurus
Sequence of entity 1 (A, B, C, D), FASTA
>8QFX_1 Angiotensin-converting enzyme, soluble form (chains A, B, C, D)
LDPGLQPGQFSADEAGAQLFAQSYQSSAEQVLFQSVAASWAHDTNITAENARRQEEAALL
SQEFAEAWGQKAKELYEPIWQQFTDPQLRRIIGAVRTLGSANLPLAKRQQYNALLSQMSR
IYSTAKVCLPQKTATCWSLDPDLTNILASSRSYAMLLFAWEGWHNAAGIPLKPLYEDFTA
LSNEAYKQDGFTDTGAYWRSWYNSPTFEDDLEHLYQQLEPLYLNLHAFVRRALHRRYGDR
YINLRGPIPAHLLGDMWAQSWENIYDMVVPFPDKPNLDVTSTMLQQGWQATHMFRVAEEF
FTSLELSPMPPEFWEGSMLEKPADGREVVCHASAWDFYNRKDFRIKQCTRVTMDQLSTVH
HEMGHIQYYLQYKDLPVSLRRGANPGFHEAIGDVLALSVSTPEHLHKIGLLDRVTNDTES
DINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPPSRYNFDWWYLRTKYQGICPPVTRN
ETHFDAGAKFHVPNVTPYIRYFVSFVLQFQFHEALCKEAGYEGPLHQCDIYRSTKAGAKL
RKVLRAGSSRPWQEVLKDMVGLDALDAQPLLKYFQLVTQWLQEQNQQNGEVLGWPEYQWH
PPLPDNYPEGIDLVTDEAEASKFVEEYD
Sequence of entity 2 (E, F, G, H), FASTA
>8QFX_2 ILE-PRO-PRO (chains E, F, G, H)
IPP

Ligands and cofactors

IDNameFormulaCopies
BMAbeta-D-mannopyranoseC6 H12 O64
MGMagnesium ionMg4
ZNZinc ionZn4
FUCalpha-L-fucopyranoseC6 H12 O52
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O613
XPE3,6,9,12,15,18,21,24,27-nonaoxanonacosane-1,29-diolC20 H42 O112

Water and common crystallization additives (CL, PGE, PEG, 1PE, PG4, ACT, EDO, 12P) are not listed.

Primary citation

Structural insights into the inhibitory mechanism of angiotensin-I-converting enzyme by the lactotripeptides IPP and VPP. Gregory, K.S., Cozier, G.E., Schwager, S.L.U. et al. FEBS Lett (2024) 598:242-251. DOI 10.1002/1873-3468.14768 · 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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