5AMC: Angiotensin-1 converting enzyme N-domain

Crystal structure of the Angiotensin-1 converting enzyme N-domain in complex with amyloid-beta fluorogenic fragment 4-10. Determined by X-ray diffraction at 1.65 Å resolution. Released 13 Jan 2016.

Method
X-ray diffraction
Resolution
1.65 Å
Organism
HOMO SAPIENS
Chains
2
Atoms
11,113
Mol. weight
150.03 kDa
Ligands
ZN, NIY, GLY
Released
13 Jan 2016

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

Secondary structure: helices and β-sheets

5AMC 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-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: 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-strand126-12834
β-strand136-13834
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-helix306-3105
α-helix311-3166
β-strand31816
β-strand333-33646
β-strand343-34646
α-helix353-37119
α-helix377-3793
α-helix385-40016
α-helix402-4076
α-helix412-4154
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 enzymeAprotein629HOMO SAPIENSP12821 (AlphaFold model)
Angiotensin-converting enzymeBprotein629HOMO SAPIENSP12821 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5AMC_1 ANGIOTENSIN-CONVERTING ENZYME (chains A)
LDPGLQPGQFSAEDAGAQLFAQSYQSSAEQVLFQSVAASWAHDTNITAENARRQEEAALL
SQEFAEAWGQKAKELYEPIWQQFTDPQLRRIIGAVRTLGSANLPLAKRQQYNALLSQMSR
IYSTAKVCLPQKTATCWSLDPDLTNILASSRSYAMLLFAWEGWHNAAGIPLKPLYEDFTA
LSNEAYKQDGFTDTGAYWRSWYNSPTFEDDLEHLYQQLEPLYLNLHAFVRRALHRRYGDR
YINLRGPIPAHLLGDMWAQSWENIYDMVVPFPDKPNLDVTSTMLQQGWQATHMFRVAEEF
FTSLELSPMPPEFWEGSMLEKPADGREVVCHASAWDFYNRKDFRIKQCTRVTMDQLSTVH
HEMGHIQYYLQYKDLPVSLRRGANPGFHEAIGDVLALSVSTPEHLHKIGLLDRVTNDTES
DINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPPSRYNFDWWYLRTKYQGICPPVTRN
ETHFDAGAKFHVPNVTPYIRYFVSFVLQFQFHEALCKEAGYEGPLHQCDIYRSTKAGAKL
RKVLRAGSSRPWQEVLKDMVGLDALDAQPLLKYFQLVTQWLQEQNQQNGEVLGWPEYQWH
PPLPDNYPEGIDLVTDEAEASKFVEEYDL
Sequence of entity 2 (B), FASTA
>5AMC_2 ANGIOTENSIN-CONVERTING ENZYME (chains B)
LDPGLQPGQFSADEAGAQLFAQSYQSSAEQVLFQSVAASWAHDTNITAENARRQEEAALL
SQEFAEAWGQKAKELYEPIWQQFTDPQLRRIIGAVRTLGSANLPLAKRQQYNALLSQMSR
IYSTAKVCLPQKTATCWSLDPDLTNILASSRSYAMLLFAWEGWHNAAGIPLKPLYEDFTA
LSNEAYKQDGFTDTGAYWRSWYNSPTFEDDLEHLYQQLEPLYLNLHAFVRRALHRRYGDR
YINLRGPIPAHLLGDMWAQSWENIYDMVVPFPDKPNLDVTSTMLQQGWQATHMFRVAEEF
FTSLELSPMPPEFWEGSMLEKPADGREVVCHASAWDFYNRKDFRIKQCTRVTMDQLSTVH
HEMGHIQYYLQYKDLPVSLRRGANPGFHEAIGDVLALSVSTPEHLHKIGLLDRVTNDTES
DINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPPSRYNFDWWYLRTKYQGICPPVTRN
ETHFDAGAKFHVPNVTPYIRYFVSFVLQFQFHEALCKEAGYEGPLHQCDIYRSTKAGAKL
RKVLRAGSSRPWQEVLKDMVGLDALDAQPLLKYFQLVTQWLQEQNQQNGEVLGWPEYQWH
PPLPDNYPEGIDLVTDEAEASKFVEEYDL

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2
NIYMeta-nitro-tyrosineC9 H10 N2 O52
GLYGlycineC2 H5 N O22

Water and common crystallization additives (P6G, PG4, PEG, CL) 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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