5AMB: Angiotensin-1 converting enzyme N-domain

Crystal structure of the Angiotensin-1 converting enzyme N-domain in complex with amyloid-beta 35-42. Determined by X-ray diffraction at 1.55 Å resolution. Released 13 Jan 2016.

Method
X-ray diffraction
Resolution
1.55 Å
Organism
HOMO SAPIENS
Chains
4
Atoms
11,095
Mol. weight
151.27 kDa
Ligands
ZN
Released
13 Jan 2016

Explore 5AMB in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5AMB contains 73 α-helices and 14 β-strands across 2 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: 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-strand126-12831
β-strand136-13831
α-helix139-1435
α-helix144-1496
α-helix153-18735
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-helix534-54613
α-helix552-5609
α-helix568-58821
α-helix590-5912
α-helix601-6044
Chain B: 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-strand126-12724
α-helix1361
β-strand137-13824
α-helix139-1435
α-helix144-1496
α-helix153-18735
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-helix353-37220
α-helix377-3793
α-helix385-40016
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

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Angiotensin-converting enzymeA, Bprotein629HOMO SAPIENSP12821 (AlphaFold model)
Amyloid beta A4 proteinP, Qprotein8HOMO SAPIENSP05067 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5AMB_1 ANGIOTENSIN-CONVERTING ENZYME (chains A, B)
LDPGLQPGQFSADEAGAQLFAQSYQSSAEQVLFQSVAASWAHDTNITAENARRQEEAALL
SQEFAEAWGQKAKELYEPIWQQFTDPQLRRIIGAVRTLGSANLPLAKRQQYNALLSQMSR
IYSTAKVCLPQKTATCWSLDPDLTNILASSRSYAMLLFAWEGWHNAAGIPLKPLYEDFTA
LSNEAYKQDGFTDTGAYWRSWYNSPTFEDDLEHLYQQLEPLYLNLHAFVRRALHRRYGDR
YINLRGPIPAHLLGDMWAQSWENIYDMVVPFPDKPNLDVTSTMLQQGWQATHMFRVAEEF
FTSLELSPMPPEFWEGSMLEKPADGREVVCHASAWDFYNRKDFRIKQCTRVTMDQLSTVH
HEMGHIQYYLQYKDLPVSLRRGANPGFHEAIGDVLALSVSTPEHLHKIGLLDRVTNDTES
DINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPPSRYNFDWWYLRTKYQGICPPVTRN
ETHFDAGAKFHVPNVTPYIRYFVSFVLQFQFHEALCKEAGYEGPLHQCDIYRSTKAGAKL
RKVLRAGSSRPWQEVLKDMVGLDALDAQPLLKYFQLVTQWLQEQNQQNGEVLGWPEYQWH
PPLPDNYPEGIDLVTDEAEASKFVEEYDL
Sequence of entity 2 (P, Q), FASTA
>5AMB_2 AMYLOID BETA A4 PROTEIN (chains P, Q)
MVGGVVIA

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2

Water and common crystallization additives (CL, PEG, P6G, PG4) are not listed.

Primary citation

The Kinetic and Structural Characterisation of Amyloid-Beta Metabolism by Human Angiotensin-1- Converting Enzyme (Ace). Larmuth, K.M., Masuyer, G., Douglas, R.G. et al. FEBS J (2016) 283:1060. DOI 10.1111/FEBS.13647 · 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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