Crystal structure of ANCE in complex with bradykinin potentiating peptide b. Determined by X-ray diffraction at 1.99 Å resolution. Released 31 Oct 2012.
Explore 4AA2 in 3D Show helices and sheets RCSB PDB PDBe
4AA2 contains 38 α-helices and 10 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 18-52 | 35 | |
| α-helix | 56-80 | 25 | |
| α-helix | 85-87 | 3 | |
| α-helix | 91-101 | 11 | |
| α-helix | 104-107 | 4 | |
| α-helix | 110-128 | 19 | |
| β-strand | 131-132 | 2 | 1 |
| β-strand | 143-144 | 2 | 1 |
| α-helix | 145-149 | 5 | |
| α-helix | 150-155 | 6 | |
| α-helix | 159-173 | 15 | |
| α-helix | 175-177 | 3 | |
| α-helix | 178-194 | 17 | |
| α-helix | 200-205 | 6 | |
| α-helix | 206-208 | 3 | |
| α-helix | 213-243 | 31 | |
| α-helix | 253 | 1 | |
| β-strand | 254-255 | 2 | 2 |
| α-helix | 256-258 | 3 | |
| α-helix | 268-270 | 3 | |
| α-helix | 271-274 | 4 | |
| α-helix | 286-291 | 6 | |
| α-helix | 296-309 | 14 | |
| α-helix | 313-316 | 4 | |
| α-helix | 317-322 | 6 | |
| β-strand | 324 | 1 | 3 |
| β-strand | 339-342 | 4 | 3 |
| β-strand | 349-352 | 4 | 3 |
| α-helix | 359-378 | 20 | |
| α-helix | 383-385 | 3 | |
| α-helix | 391-405 | 15 | |
| α-helix | 408-413 | 6 | |
| α-helix | 424-438 | 15 | |
| α-helix | 441-456 | 16 | |
| α-helix | 462-464 | 3 | |
| α-helix | 465-477 | 13 | |
| β-strand | 479-480 | 2 | 2 |
| β-strand | 485-486 | 2 | 4 |
| α-helix | 492-494 | 3 | |
| α-helix | 496-499 | 4 | |
| α-helix | 505-524 | 20 | |
| α-helix | 537-539 | 3 | |
| α-helix | 546-556 | 11 | |
| α-helix | 564-572 | 9 | |
| α-helix | 580-599 | 20 | |
| α-helix | 607-609 | 3 | |
| β-strand | 612-613 | 2 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8 | 1 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Angiotensin-converting enzyme | A | protein | 598 | DROSOPHILA MELANOGASTER | Q10714 (AlphaFold model) |
| Bradykinin-potentiating peptide B | P | protein | 11 | GLOYDIUS BLOMHOFFI | P01021 (AlphaFold model) |
>4AA2_1 ANGIOTENSIN-CONVERTING ENZYME (chains A) ALVKEEIQAKEYLENLNKELAKRTNVETEAAWAYGSNITDENEKKKNEISAELAKFMKEV ASDTTKFQWRSYQSEDLKRQFKALTKLGYAALPEDDYAELLDTLSAMESNFAKVKVCDYK DSTKCDLALDPEIEEVISKSRDHEELAYYWREFYDKAGTAVRSQFERYVELNTKAAKLNN FTSGAEAWLDEYEDDTFEQQLEDIFADIRPLYQQIHGYVRFRLRKHYGDAVVSETGPIPM HLLGNMWAQQWSEIADIVSPFPEKPLVDVSAEMEKQGYTPLKMFQMGDDFFTSMNLTKLP QDFWDKSIIEKPTDGRDLVCHASAWDFYLTDDVRIKQCTRVTQDQLFTVHHELGHIQYFL QYQHQPFVYRTGANPGFHEAVGDVLSLSVSTPKHLEKIGLLKDYVRDDEARINQLFLTAL DKIVFLPFAFTMDKYRWSLFRGEVDKANWNCAFWKLRDEYSGIEPPVVRSEKDFDAPAKY HISADVEYLRYLVSFIIQFQFYKSACIKAGQYDPDNVELPLDNCDIYGSAAAGAAFHNML SMGASKPWPDALEAFNGERIMSGKAIAEYFEPLRVWLEAENIKNNVHIGWTTSNKCVS
>4AA2_2 BRADYKININ-POTENTIATING PEPTIDE B (chains P) EGLPPRPKIPP
Structural Basis of Peptide Recognition by the Angiotensin-I Converting Enzyme Homologue Ance from Drosophila Melanogaster. Akif, M., Masuyer, G., Bingham, R.J. et al. FEBS J (2012) 279:4525. DOI 10.1111/FEBS.12038 · PubMed
Other PDB entries of the same protein (UniProt Q10714 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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