4UFA: Angiotensin-1 converting enzyme N-domain

Crystal structure of the Angiotensin-1 converting enzyme N-domain in complex with Ac-SD. Determined by X-ray diffraction at 1.8 Å resolution. Released 7 Oct 2015.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
HOMO SAPIENS
Chains
2
Atoms
10,977
Mol. weight
149.8 kDa
Ligands
NAG, ZN, ASP, SAC
Released
7 Oct 2015

Explore 4UFA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4UFA 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-helix280-2867
α-helix290-30314
α-helix307-3104
α-helix311-3166
β-strand31813
β-strand333-33643
β-strand343-34643
α-helix353-37220
α-helix377-3793
α-helix385-40016
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-helix568-58720
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-helix353-37220
α-helix377-3793
α-helix385-40016
α-helix402-4076
α-helix412-4143
α-helix419-43214
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)
Sequence of entity 1 (A, B), FASTA
>4UFA_1 ANGIOTENSIN-CONVERTING ENZYME (chains A, B)
LDPGLQPGQFSADEAGAQLFAQSYQSSAEQVLFQSVAASWAHDTNITAENARRQEEAALL
SQEFAEAWGQKAKELYEPIWQQFTDPQLRRIIGAVRTLGSANLPLAKRQQYNALLSQMSR
IYSTAKVCLPQKTATCWSLDPDLTNILASSRSYAMLLFAWEGWHNAAGIPLKPLYEDFTA
LSNEAYKQDGFTDTGAYWRSWYNSPTFEDDLEHLYQQLEPLYLNLHAFVRRALHRRYGDR
YINLRGPIPAHLLGDMWAQSWENIYDMVVPFPDKPNLDVTSTMLQQGWQATHMFRVAEEF
FTSLELSPMPPEFWEGSMLEKPADGREVVCHASAWDFYNRKDFRIKQCTRVTMDQLSTVH
HEMGHIQYYLQYKDLPVSLRRGANPGFHEAIGDVLALSVSTPEHLHKIGLLDRVTNDTES
DINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPPSRYNFDWWYLRTKYQGICPPVTRN
ETHFDAGAKFHVPNVTPYIRYFVSFVLQFQFHEALCKEAGYEGPLHQCDIYRSTKAGAKL
RKVLRAGSSRPWQEVLKDMVGLDALDAQPLLKYFQLVTQWLQEQNQQNGEVLGWPEYQWH
PPLPDNYPEGIDLVTDEAEASKFVEEYDL

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O62
ZNZinc ionZn2
ASPAspartic acidC4 H7 N O42
SACN-acetyl-serineC5 H9 N O42

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

Primary citation

Structural Basis of Ac-Sdkp Hydrolysis by Angiotensin-I Converting Enzyme. Masuyer, G., Douglas, R.G., Sturrock, E.D. et al. Sci Rep (2015) 5:13742. DOI 10.1038/SREP13742 · 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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